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ATP + G protein-coupled receptor
ADP + phosphorylated G protein-coupled receptor
ATP + rhodopsin
ADP + phosphorylated rhodopsin
dark-adapted and light-activated rhodopsin in urea-washed rod outer segment membranes
-
-
?
ATP + [beta-adrenergic receptor]
ADP + phospho-[beta-adrenergic receptor]
-
-
-
?
ATP + alpha2-adrenergic receptor
ADP + phospho-alpha2-adrenergic receptor
ATP + alpha2A-adrenergic receptor
ADP + phosphorylated alpha2A-adrenergic receptor
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
ATP + beta-adrenergic receptor
ADP + phosphorylated beta-adrenergic receptor
-
agonist-activated receptor substrate
-
-
?
ATP + dopamine D3 receptor
ADP + phosphorylated dopamine D3 receptor
ATP + G protein-coupled receptor
ADP + phosphorylated G protein-coupled receptor
ATP + LEESSSSDHAERPPG
?
-
-
-
-
?
ATP + micro-opioid receptor
ADP + phosphorylated micro-opioid receptor
-
mutant C221V GRK2 shows slightly higher effect on morphine-induced internalization of the micro-opioid receptor compared to the wild-type GRK2, while the effects of mutants L271G, L273Y, and L336F are reduced, overview
-
-
?
ATP + muscarinic acetylcholine receptor
ADP + phospho-muscarinic acetylcholine receptor
-
agonist-dependent phosphorylation, subtype 2
-
-
?
ATP + muscarinic cholinergic receptor
ADP + phospho-muscarinic cholinergic receptor
ATP + peptide
ADP + phosphopeptide
ATP + platelet-derived growth factor receptor-beta
ADP + phosphorylated platelet-derived growth factor receptor-beta
ATP + protein
ADP + phosphoprotein
specifically phosphorylates the agonist-occupied form of the beta-adrenergic and related G protein-coupled receptors
-
-
?
ATP + rhodopsin
ADP + phosphorhodopsin
ATP + rhodopsin
ADP + phosphorylated rhodopsin
ATP + RRRAEAAASAAA
ADP + RRRAEAAApSAAA
-
-
-
-
?
ATP + RRRAEASAA
ADP + RRRAEApSAA
-
poor peptide substrate
-
-
?
ATP + RRRASAAASAA
?
-
poor peptide substrate
-
-
?
ATP + RRRASASAA
?
-
poor peptide substrate
-
-
?
ATP + RRRASpAAASAA
ADP + RRRASpAAASpAA
-
poor peptide substrate, higher catalytic efficiency than RRRASAAASAA
-
-
?
ATP + RRRASpASAA
?
-
poor peptide substrate
-
-
?
ATP + Smoothened protein
ADP + phopshorylated Smoothened
-
a seven-transmembrane signaling protein
-
-
?
ATP + Smoothened protein
ADP + phosphorylated Smoothened
-
GRK2 promotes smoothened signal transduction involved in regulation of cellular proliferation and differentiation through activation of the transcription factor Gli, overview
-
-
?
ATP + tubulin
ADP + phosphorylated tubulin
-
-
-
-
?
ATP + [beta-adrenergic receptor]
ADP + phospho-[beta-adrenergic receptor]
-
-
-
-
?
GTP + beta-adrenergic receptor
GDP + phospho-beta-adrenergic receptor
-
agonist-occupied form of beta-AR from hamster lung, GTP can substitute ATP, 2% as effective as ATP
-
?
histamine H2 receptor + ATP
phosphorylated histamine H2 receptor + ADP
-
-
-
-
?
additional information
?
-
ATP + G protein-coupled receptor
ADP + phosphorylated G protein-coupled receptor
-
-
-
?
ATP + G protein-coupled receptor
ADP + phosphorylated G protein-coupled receptor
GRK2 performs desensitization of the ligand-activated receptor by phosphorylation
-
-
?
ATP + alpha2-adrenergic receptor
ADP + phospho-alpha2-adrenergic receptor
-
-
-
-
?
ATP + alpha2-adrenergic receptor
ADP + phospho-alpha2-adrenergic receptor
-
dependent on agonist occupancy by (-)-epinephrine, equally effective as beta-adrenergic receptor, incorporation of 7-8 mol phosphate/mol receptor
-
-
?
ATP + alpha2-adrenergic receptor
ADP + phospho-alpha2-adrenergic receptor
-
agonist-induced phosphorylation
-
-
?
ATP + alpha2-adrenergic receptor
ADP + phospho-alpha2-adrenergic receptor
-
from human platelets
-
-
?
ATP + alpha2A-adrenergic receptor
ADP + phosphorylated alpha2A-adrenergic receptor
-
-
-
-
?
ATP + alpha2A-adrenergic receptor
ADP + phosphorylated alpha2A-adrenergic receptor
-
interaction with GRK2 via the second and third intracellular loop of the receptor, determination of regions required for specific interaction and phosphorylation activity utilizing recombinant GST-tagged wild-type and several mutant alpha2A AR substrates, residues R225, R226, R218, K320, R322, and K358 are important, overview
-
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
-
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
-
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
-
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
phosphorylation sites
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
phosphorylation sites are located mainly at the C-terminal tail of the receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
incorporation of 7-8 mol phosphate/mol receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
incorporation of about 9 mol phosphate/mol receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
beta2-adrenergic receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
beta2-adrenergic receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
beta2-adrenergic receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
beta2-adrenergic receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
beta2-adrenergic receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
beta2-adrenergic receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
beta2-adrenergic receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
beta2-adrenergic receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
specifically phosphorylates the agonist-occupied form of the receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
specifically phosphorylates the agonist-occupied form of the receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
specifically phosphorylates the agonist-occupied form of the receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
specifically phosphorylates the agonist-occupied form of the receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
specifically phosphorylates the agonist-occupied form of the receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
specifically phosphorylates the agonist-occupied form of the receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
specifically phosphorylates the agonist-occupied form of the receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
specifically phosphorylates the agonist-occupied form of the receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
specifically phosphorylates the agonist-occupied form of the receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
specifically phosphorylates the agonist-occupied form of the receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
specifically phosphorylates the agonist-occupied form of the receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
specifically phosphorylates the agonist-occupied form of the receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
specifically phosphorylates the agonist-occupied form of the receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
specifically phosphorylates the agonist-occupied form of the receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
specifically phosphorylates the agonist-occupied form of the receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
specifically phosphorylates the agonist-occupied form of the receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
specifically phosphorylates the agonist-occupied form of the receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
similar rates of beta-ARK 1 and 2 for beta2-adrenergic receptor phosphorylation
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
human beta2-adrenergic receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
human beta2-adrenergic receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
human beta2-adrenergic receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
at a similar rate as muscarinic cholinergic receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
at a similar rate as alpha2-adrenergic receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
substrates: wild-type and mutants of beta2-AR, synergistic action of beta-ARK and cAMP-dependent protein kinase depends on the palmitoylation state of the receptor, putative phosphorylation sites of beta2-AR
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
incorporation of up to 5 mol phosphate/mol receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
incorporation of up to 5 mol phosphate/mol receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
beta-ARK 1, substrate specificity, the overall topological structure of the activated receptor plays a key role in regulating signal-dependent receptor phosphorylation
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
beta-ARK 2 has a 25% lower specific activity than beta-ARK 1 towards rhodopsin and beta2-AR
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
incorporation of 6-8 mol phosphate/mol receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
beta-AR from Sf9 cells
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
beta-AR from hamster lung
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
beta-AR from hamster lung
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
beta-AR from hamster lung
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
beta-AR from hamster lung
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
beta-AR from hamster lung
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
beta-AR from hamster lung
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
beta-AR is a much better substrate than rhodopsin
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
beta-AR is a much better substrate than rhodopsin
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
beta-AR is a much better substrate than rhodopsin
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
natural substrate: beta2-adrenergic receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
natural substrate: beta2-adrenergic receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
beta-ARK 1 and 2 may have a similar substrate specificity in vivo
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
regulation of the beta-AR function in vivo
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
desensitization of beta-adrenergic receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
desensitization of beta-adrenergic receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
plays, together with cAMP-dependent protein kinase, an important role in agonist-promoted receptor desensitization, coordinated regulatory mechanism involving sequential depalmitoylation and phosphorylation of the beta2-AR by the two kinases
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
agonist-occupied form of the receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
agonist-occupied form of the receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
agonist-occupied form of the receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
agonist-occupied form of the receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
agonist-occupied form of the receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
agonist-occupied form of the receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
agonist-occupied form of the receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
agonist-occupied form of the receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
agonist-occupied form of the receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
agonist-occupied form of the receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
agonist-occupied form of the receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
agonist-occupied form of the receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
agonist-occupied form of the receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
agonist-occupied form of the receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
agonist-occupied form of the receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
involved in homologous desensitization of beta-adrenergic receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
involved in homologous desensitization of beta-adrenergic receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
involved in homologous desensitization of beta-adrenergic receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
involved in homologous desensitization of beta-adrenergic receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
involved in homologous desensitization of beta-adrenergic receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
involved in homologous desensitization of beta-adrenergic receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
involved in homologous desensitization of beta-adrenergic receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
involved in homologous desensitization of beta-adrenergic receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
involved in homologous desensitization of beta-adrenergic receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
involved in homologous desensitization of beta-adrenergic receptor
-
?
ATP + dopamine D3 receptor
ADP + phosphorylated dopamine D3 receptor
-
-
-
-
?
ATP + dopamine D3 receptor
ADP + phosphorylated dopamine D3 receptor
-
the receptor is activated by GRK2 and GRK3 phosphorylation involving beta-arrestins, GRK-mediated regulation of receptor-filamin complex stability and receptor-G protein signaling potential, GRK2 reduces the dopamine D3 receptor signaling, overview
-
-
?
ATP + G protein-coupled receptor
ADP + phosphorylated G protein-coupled receptor
-
-
-
-
?
ATP + G protein-coupled receptor
ADP + phosphorylated G protein-coupled receptor
-
desensitization by GRK2 of the ligand-activated receptor
-
-
?
ATP + G protein-coupled receptor
ADP + phosphorylated G protein-coupled receptor
-
desensitization of agonist-activated receptor
-
-
?
ATP + muscarinic cholinergic receptor
ADP + phospho-muscarinic cholinergic receptor
-
in vitro as good as beta-adrenergic receptor, phosphorylation depends on the presence of a muscarinic agonist ligand, not merely receptor occupancy, the agonist induces a conformational change, which allows phosphorylation, phosphorylation sites: 70% Ser- and 30% Thr-residues, incorporation of 3-4 mol phosphate/mol receptor
-
-
?
ATP + muscarinic cholinergic receptor
ADP + phospho-muscarinic cholinergic receptor
-
from chick heart
-
-
?
ATP + peptide
ADP + phosphopeptide
-
beta-ARK 1 and 2 prefer peptide substrates with acidic amino acids N-terminal to a Ser-residue
-
-
?
ATP + peptide
ADP + phosphopeptide
-
beta-ARK 1 prefers peptides containing acidic residues on the N-terminal side of a serine or threonine, presence of activated receptor enhances peptide phosphorylation
-
-
?
ATP + peptide
ADP + phosphopeptide
-
e.g. Leu-Glu-Glu-Ser-Ser-Ser-Ser-Asp-His-Ala-Glu-Arg-Pro-Pro-Gly or Arg-Arg-Arg-Glu-Glu-Glu-Glu-Glu-Ser-Ala-Ala-Ala, role of acidic amino acids in peptide substrates, preference for negatively charged amino acids localized to the N-terminal side of a Ser- or Thr-residue, Ser-containing peptides are 4fold better than Thr-containing
-
-
?
ATP + peptide
ADP + phosphopeptide
-
synthetic
-
-
?
ATP + platelet-derived growth factor receptor-beta
ADP + phosphorylated platelet-derived growth factor receptor-beta
-
feedback inhibition mechanism, overview
-
-
?
ATP + platelet-derived growth factor receptor-beta
ADP + phosphorylated platelet-derived growth factor receptor-beta
-
active with the wild-type and mutant Y740F/Y751F PDGFRbeta, GRK2 phosphorylation desensitizes the PDGF receptor-beta, feedback inhibition mechanism, overview
-
-
?
ATP + rhodopsin
ADP + phosphorhodopsin
-
beta-ARK 2 has a 25% lower specific activity than beta-ARK 1 towards rhodopsin and beta2-AR
-
?
ATP + rhodopsin
ADP + phosphorhodopsin
beta-AR is a much better substrate than rhodopsin
-
?
ATP + rhodopsin
ADP + phosphorhodopsin
-
beta-AR is a much better substrate than rhodopsin
-
?
ATP + rhodopsin
ADP + phosphorhodopsin
-
beta-AR is a much better substrate than rhodopsin
-
?
ATP + rhodopsin
ADP + phosphorhodopsin
-
beta-AR is a much better substrate than rhodopsin
-
?
ATP + rhodopsin
ADP + phosphorhodopsin
-
light-dependent, actual substrate: light-bleached rhodopsin
-
?
ATP + rhodopsin
ADP + phosphorhodopsin
light-dependent, actual substrate: light-bleached rhodopsin
-
?
ATP + rhodopsin
ADP + phosphorhodopsin
-
light-dependent, actual substrate: light-bleached rhodopsin
-
?
ATP + rhodopsin
ADP + phosphorhodopsin
-
light-dependent, actual substrate: light-bleached rhodopsin
-
?
ATP + rhodopsin
ADP + phosphorhodopsin
-
light-dependent, actual substrate: light-bleached rhodopsin
-
?
ATP + rhodopsin
ADP + phosphorhodopsin
-
light-dependent, actual substrate: light-bleached rhodopsin
-
?
ATP + rhodopsin
ADP + phosphorhodopsin
-
light-dependent, actual substrate: light-bleached rhodopsin
-
?
ATP + rhodopsin
ADP + phosphorhodopsin
-
light-dependent, actual substrate: light-bleached rhodopsin
-
?
ATP + rhodopsin
ADP + phosphorhodopsin
-
light-dependent, actual substrate: light-bleached rhodopsin
-
?
ATP + rhodopsin
ADP + phosphorhodopsin
-
light-dependent, actual substrate: light-bleached rhodopsin
-
?
ATP + rhodopsin
ADP + phosphorhodopsin
-
incorporation of 0.15 mol phosphate/mol rhodopsin
-
?
ATP + rhodopsin
ADP + phosphorhodopsin
-
incorporation of 0.15 mol phosphate/mol rhodopsin
-
?
ATP + rhodopsin
ADP + phosphorhodopsin
-
in form of bovine rod outer segments
-
?
ATP + rhodopsin
ADP + phosphorhodopsin
in form of bovine rod outer segments
-
?
ATP + rhodopsin
ADP + phosphorhodopsin
-
in form of bovine rod outer segments
-
?
ATP + rhodopsin
ADP + phosphorhodopsin
-
in form of bovine rod outer segments
-
?
ATP + rhodopsin
ADP + phosphorhodopsin
-
in form of bovine rod outer segments
-
?
ATP + rhodopsin
ADP + phosphorhodopsin
-
in form of bovine rod outer segments
-
?
ATP + rhodopsin
ADP + phosphorhodopsin
-
in form of bovine rod outer segments
-
?
ATP + rhodopsin
ADP + phosphorhodopsin
-
in form of bovine rod outer segments
-
?
ATP + rhodopsin
ADP + phosphorhodopsin
-
in form of bovine rod outer segments
-
?
ATP + rhodopsin
ADP + phosphorhodopsin
-
in form of bovine rod outer segments
-
?
ATP + rhodopsin
ADP + phosphorhodopsin
-
in form of bovine rod outer segments
-
?
ATP + rhodopsin
ADP + phosphorhodopsin
-
in form of bovine rod outer segments
-
?
ATP + rhodopsin
ADP + phosphorhodopsin
-
in form of bovine rod outer segments
-
?
ATP + rhodopsin
ADP + phosphorhodopsin
-
metarhodopsin II, poor substrate
-
?
ATP + rhodopsin
ADP + phosphorylated rhodopsin
-
-
-
-
?
ATP + rhodopsin
ADP + phosphorylated rhodopsin
-
light-activated rhodopsin
-
-
?
ATP + rhodopsin
ADP + phosphorylated rhodopsin
-
light-activated rhodopsin, both isozymes ARK1 and ARK2 prefer acidic amino acids N-terminal to a serine for phosphorylation
-
-
?
ATP + RRREEEEESAAA
?
-
-
-
-
?
ATP + RRREEEEESAAA
?
-
nonreceptor peptide substrate
-
-
?
ATP + RRREEEEESAAA
?
-
good peptide substrate, but the activated receptor is a much better substrate
-
-
?
additional information
?
-
-
enzyme is important in mediating rapid agonist-specific desensitization
-
-
?
additional information
?
-
enzyme is important in mediating rapid agonist-specific desensitization
-
-
?
additional information
?
-
-
domain structure
-
-
?
additional information
?
-
-
domain structure
-
-
?
additional information
?
-
domain structure
-
-
?
additional information
?
-
-
beta-ARK interacts rapidly with a high affinity binding site present in salt-stripped rat liver microsomal membranes, modulation of binding of enzyme
-
-
?
additional information
?
-
-
mechanism and significance of the PH-domain function
-
-
?
additional information
?
-
-
phosphorylates G protein coupled receptors in an agonist-dependent manner
-
-
?
additional information
?
-
-
phosphorylates G protein coupled receptors in an agonist-dependent manner
-
-
?
additional information
?
-
-
role of the PH domain, ligand binding characteristics of the PH domain, distinct role for each ligand, i.e. betagamma subunits of G proteins and phosphatidylinositol 4,5-bisphosphate, in enzyme-mediated receptor phosphorylation
-
-
?
additional information
?
-
-
not: alpha1-adrenergic receptor
-
-
?
additional information
?
-
-
rhodopsin kinase, EC 2.7.11.14, is also capable of beta-adrenergic receptor phosphorylation
-
-
?
additional information
?
-
-
very poor substrates: casein, phosvitin
-
-
?
additional information
?
-
-
beta-ARK is probably a general adenylate cyclase-coupled receptor kinase
-
-
?
additional information
?
-
-
beta-ARK 1 is a key regulatory enzyme involved in the regulation of G protein-coupled receptors which associate with microsomal and plasma membranes
-
-
?
additional information
?
-
-
plays a pivotal role in phosphorylating and desensitizing G protein-coupled receptors by vitue of pleckstrin homology domain-mediated membrane translocation
-
-
?
additional information
?
-
-
beta-ARK activity is regulated by endogenous G proteins in different intracellular locations
-
-
?
additional information
?
-
-
phosphorylates and regulates receptors coupled to either stimulation or inhibition of adenylate cyclase
-
-
?
additional information
?
-
-
phosphorylates and regulates receptors coupled to either stimulation or inhibition of adenylate cyclase
-
-
?
additional information
?
-
-
dopamine D3 receptor binds to G proteins, the coupling is regulated by the filamin expression level
-
-
?
additional information
?
-
-
GRK2 is involved in A2 adenosine receptor response to agonists
-
-
?
additional information
?
-
-
GRK2 regulation mechanism of ERK activation involving interaction with mitogen-activated protein kinase, GRK2 diminishes the level of activating phosphorylation of ERK by CCL2 binding to chemokine receptor CCR2 in endothelial cells
-
-
?
additional information
?
-
-
phosphorylation of heptahelical receptors by GRK2 is a universal regulatory mehanism leading to desensitization of G protein signaling and to the activation of alternative signaling pathways
-
-
?
additional information
?
-
-
peptide phosphorylation study
-
-
?
additional information
?
-
-
the enzyme contains regulatory sites for Ca2+/calmodulin, protein kinase C, and clathrin
-
-
?
additional information
?
-
-
GRK2 regulates 7TM G-protein-coupled receptor activity, GRK2 promotes the association between active Smoothened and beta-arrestin 2, overview
-
-
?
additional information
?
-
-
carboxyl-terminus of GRK2 interacts with Hsp90. Reactive oxygen species (ROS)-mediated mitochrondrial localisation of GRK2 is dependent on Hsp90 binding
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + G protein-coupled receptor
ADP + phosphorylated G protein-coupled receptor
GRK2 performs desensitization of the ligand-activated receptor by phosphorylation
-
-
?
ATP + [beta-adrenergic receptor]
ADP + phospho-[beta-adrenergic receptor]
-
-
-
?
ATP + alpha2A-adrenergic receptor
ADP + phosphorylated alpha2A-adrenergic receptor
-
-
-
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
ATP + beta-adrenergic receptor
ADP + phosphorylated beta-adrenergic receptor
-
agonist-activated receptor substrate
-
-
?
ATP + dopamine D3 receptor
ADP + phosphorylated dopamine D3 receptor
-
the receptor is activated by GRK2 and GRK3 phosphorylation involving beta-arrestins, GRK-mediated regulation of receptor-filamin complex stability and receptor-G protein signaling potential, GRK2 reduces the dopamine D3 receptor signaling, overview
-
-
?
ATP + G protein-coupled receptor
ADP + phosphorylated G protein-coupled receptor
ATP + platelet-derived growth factor receptor-beta
ADP + phosphorylated platelet-derived growth factor receptor-beta
-
feedback inhibition mechanism, overview
-
-
?
ATP + protein
ADP + phosphoprotein
specifically phosphorylates the agonist-occupied form of the beta-adrenergic and related G protein-coupled receptors
-
-
?
ATP + rhodopsin
ADP + phosphorylated rhodopsin
-
light-activated rhodopsin
-
-
?
ATP + Smoothened protein
ADP + phosphorylated Smoothened
-
GRK2 promotes smoothened signal transduction involved in regulation of cellular proliferation and differentiation through activation of the transcription factor Gli, overview
-
-
?
histamine H2 receptor + ATP
phosphorylated histamine H2 receptor + ADP
-
-
-
-
?
additional information
?
-
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
natural substrate: beta2-adrenergic receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
natural substrate: beta2-adrenergic receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
beta-ARK 1 and 2 may have a similar substrate specificity in vivo
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
regulation of the beta-AR function in vivo
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
desensitization of beta-adrenergic receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
desensitization of beta-adrenergic receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
plays, together with cAMP-dependent protein kinase, an important role in agonist-promoted receptor desensitization, coordinated regulatory mechanism involving sequential depalmitoylation and phosphorylation of the beta2-AR by the two kinases
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
agonist-occupied form of the receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
agonist-occupied form of the receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
agonist-occupied form of the receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
agonist-occupied form of the receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
agonist-occupied form of the receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
agonist-occupied form of the receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
agonist-occupied form of the receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
agonist-occupied form of the receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
agonist-occupied form of the receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
agonist-occupied form of the receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
agonist-occupied form of the receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
agonist-occupied form of the receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
agonist-occupied form of the receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
agonist-occupied form of the receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
agonist-occupied form of the receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
involved in homologous desensitization of beta-adrenergic receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
involved in homologous desensitization of beta-adrenergic receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
involved in homologous desensitization of beta-adrenergic receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
involved in homologous desensitization of beta-adrenergic receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
involved in homologous desensitization of beta-adrenergic receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
involved in homologous desensitization of beta-adrenergic receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
involved in homologous desensitization of beta-adrenergic receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
involved in homologous desensitization of beta-adrenergic receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
involved in homologous desensitization of beta-adrenergic receptor
-
?
ATP + beta-adrenergic receptor
ADP + phospho-beta-adrenergic receptor
-
involved in homologous desensitization of beta-adrenergic receptor
-
?
ATP + G protein-coupled receptor
ADP + phosphorylated G protein-coupled receptor
-
desensitization by GRK2 of the ligand-activated receptor
-
-
?
ATP + G protein-coupled receptor
ADP + phosphorylated G protein-coupled receptor
-
desensitization of agonist-activated receptor
-
-
?
additional information
?
-
-
enzyme is important in mediating rapid agonist-specific desensitization
-
-
?
additional information
?
-
enzyme is important in mediating rapid agonist-specific desensitization
-
-
?
additional information
?
-
-
beta-ARK is probably a general adenylate cyclase-coupled receptor kinase
-
-
?
additional information
?
-
-
beta-ARK 1 is a key regulatory enzyme involved in the regulation of G protein-coupled receptors which associate with microsomal and plasma membranes
-
-
?
additional information
?
-
-
plays a pivotal role in phosphorylating and desensitizing G protein-coupled receptors by vitue of pleckstrin homology domain-mediated membrane translocation
-
-
?
additional information
?
-
-
beta-ARK activity is regulated by endogenous G proteins in different intracellular locations
-
-
?
additional information
?
-
-
phosphorylates and regulates receptors coupled to either stimulation or inhibition of adenylate cyclase
-
-
?
additional information
?
-
-
phosphorylates and regulates receptors coupled to either stimulation or inhibition of adenylate cyclase
-
-
?
additional information
?
-
-
dopamine D3 receptor binds to G proteins, the coupling is regulated by the filamin expression level
-
-
?
additional information
?
-
-
GRK2 is involved in A2 adenosine receptor response to agonists
-
-
?
additional information
?
-
-
GRK2 regulation mechanism of ERK activation involving interaction with mitogen-activated protein kinase, GRK2 diminishes the level of activating phosphorylation of ERK by CCL2 binding to chemokine receptor CCR2 in endothelial cells
-
-
?
additional information
?
-
-
phosphorylation of heptahelical receptors by GRK2 is a universal regulatory mehanism leading to desensitization of G protein signaling and to the activation of alternative signaling pathways
-
-
?
additional information
?
-
-
GRK2 regulates 7TM G-protein-coupled receptor activity, GRK2 promotes the association between active Smoothened and beta-arrestin 2, overview
-
-
?
additional information
?
-
-
carboxyl-terminus of GRK2 interacts with Hsp90. Reactive oxygen species (ROS)-mediated mitochrondrial localisation of GRK2 is dependent on Hsp90 binding
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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4-(3-((2,6-bis(trifluoromethyl)benzyl)carbamoyl)-4-fluorophenyl)-N-(1H-indazol-5-yl)-6-methyl-2-oxo-1,2,3,4-tetrahydropyrimidine-5-carboxamide
-
4-(3-((2,6-dichlorobenzyl)carbamoyl)-4-fluorophenyl)-N-(1H-indazol-5-yl)-6-methyl-2-oxo-1,2,3,4-tetrahydropyrimidine-5-carboxamide
-
4-(3-((2,6-difluorobenzyl)carbamoyl)-4-fluorophenyl)-N-(1H-indazol-5-yl)-6-methyl-2-oxo-1,2,3,4-tetrahydropyrimidine-5-carboxamide
-
4-(3-((2,6-dimethoxybenzyl)carbamoyl)-4-fluorophenyl)-N-(1Hindazol-5-yl)-6-methyl-2-oxo-1,2,3,4-tetrahydropyrimidine-5-carboxamide
-
4-(3-((2,6-dimethylbenzyl)carbamoyl)-4-fluorophenyl)-N-(1H-indazol-5-yl)-6-methyl-2-oxo-1,2,3,4-tetrahydropyrimidine-5 carboxamide
-
4-(3-((2,6-dimethylbenzyl)carbamoyl)-4-fluorophenyl)-N-(1H-indazol-5-yl)-N,6-dimethyl-2-oxo-1,2,3,4-tetrahydropyrimidine-5-carboxamide
-
4-(3-((2,6-dimethylphenethyl)carbamoyl)-4-fluorophenyl)-N-(1H-indazol-5-yl)-6-methyl-2-oxo-1,2,3,4-tetrahydropyrimidine-5-carboxamide
-
4-(3-((3,5-bis(trifluoromethyl)benzyl)carbamoyl)-4-fluorophenyl)-N-(1H-indazol-5-yl)-6-methyl-2-oxo-1,2,3,4-tetrahydropyrimidine-5-carboxamide
-
4-(3-(2-((2,6-bis(trifluoromethyl)benzyl)amino)-2-oxoethyl)-4-fluorophenyl)-N-(1H-indazol-5-yl)-6-methyl-2-oxo-1,2,3,4-tetrahydropyrimidine-5-carboxamide
-
4-(3-(2-((2,6-dimethoxybenzyl)amino)-2-oxoethyl)-4-fluorophenyl)-N-(1H-indazol-5-yl)-6-methyl-2-oxo-1,2,3,4-tetrahydropyrimidine-5-carboxamide
-
4-(3-(2-((2,6-dimethylbenzyl)amino)-2-oxoethyl)-4-fluorophenyl)-N-(1H-indazol-5-yl)-6-methyl-2-oxo-1,2,3,4-tetrahydropyrimidine-5-carboxamide
-
4-(3-(benzylcarbamoyl)-4-fluorophenyl)-N-(1H-indazol-5-yl)-6-methyl-2-oxo-1,2,3,4-tetrahydropyrimidine-5-carboxamide
-
4-(4-fluoro-3-(((3-methylpyridin-2-yl)methyl)carbamoyl)phenyl)-N-(1H-indazol-5-yl)-6-methyl-2-oxo-1,2,3,4-tetrahydropyrimidine-5-carboxamide
-
4-(4-fluoro-3-((2-(pyridin-2-yl)ethyl)carbamoyl)phenyl)-N-(1H-indazol-5-yl)-6-methyl-2-oxo-1,2,3,4-tetrahydropyrimidine-5-carboxamide
-
4-(4-fluoro-3-((2-(pyridin-4-yl)ethyl)carbamoyl)phenyl)-N-(1H-indazol-5-yl)-6-methyl-2-oxo-1,2,3,4-tetrahydropyrimidine-5-carboxamide
-
4-(4-fluoro-3-((2-methoxybenzyl)carbamoyl)phenyl)-N-(1H-indazol-5-yl)-6-methyl-2-oxo-1,2,3,4-tetrahydropyrimidine-5-carboxamide
-
4-(4-fluoro-3-((3-fluorobenzyl)carbamoyl)phenyl)-N-(1H-indazol-5-yl)-6-methyl-2-oxo-1,2,3,4-tetrahydropyrimidine-5-carboxamide
-
4-(4-fluoro-3-((3-methoxybenzyl)carbamoyl)phenyl)-N-(1H-indazol-5-yl)-6-methyl-2-oxo-1,2,3,4-tetrahydropyrimidine-5-carboxamide
-
4-(4-fluoro-3-((4-methoxybenzyl)carbamoyl)phenyl)-N-(1H-indazol-5-yl)-6-methyl-2-oxo-1,2,3,4-tetrahydropyrimidine-5-carboxamide
-
4-(4-fluoro-3-((isoquinolin-1-ylmethyl)carbamoyl)phenyl)-N-(1H-indazol-5-yl)-6-methyl-2-oxo-1,2,3,4-tetrahydropyrimidine-5-carboxamide
-
4-(4-fluoro-3-((pyridin-2-ylmethyl)carbamoyl)phenyl)-N-(1H-indazol-5-yl)-6-methyl-2-oxo-1,2,3,4-tetrahydropyrimidine-5-carboxamide
-
4-(4-fluoro-3-(methylcarbamoyl)phenyl)-N-(1H-indazol-5-yl)-6-methyl-2-oxo-1,2,3,4-tetrahydropyrimidine-5-carboxamide
-
5-(5-((1H-indazol-5-yl)carbamoyl)-6-methyl-2-oxo-1,2,3,4-tetrahydropyrimidin-4-yl)-2-fluorobenzoic acid
-
N-(benzo[d][1,3]dioxol-5-yl)-4-(4-fluoro-3-((pyridin-2-ylmethyl)-carbamoyl)phenyl)-6-methyl-2-oxo-1,2,3,4-tetrahydropyrimidine-5-carboxamide
-
4-amino-1-tert-butyl-3-(1'-naphthyl)pyrrazolo[3,4-d]pyrimidine
-
i.e. 1-Na-PP1, inhibits mutant C221V mediated morphine-induced internalization of the micro-opioid receptor, but not wild-type GRK2 and mutant L271G activities
alpha2-adrenergic antagonist
-
co-incubation completely blocks phosphorylation of alpha2-adrenergic receptor
-
atropine
-
receptor antagonist
Chloropromazine
-
IC50: 0.043 mM
chondroitin sulfate B
-
weak
chondroitin sulfate C
-
less inhibitory than heparin
D-glucosamine 2,6-disulfate
-
inhibits in the millimolar range, weak, IC50: 7.3 mM with rhodopsin as substrate
D-sphingosine
-
IC50: 0.027 mM
Dextran sulfate
-
strong, IC50: 0.00015 mM with rhodopsin as substrate
-
heparan sulfate
-
less inhibitory than heparin
Inositol hexaphosphate
-
weak, IC50: 3.6 mM with rhodopsin as substrate
McN-A343
-
weak, partial antagonist
NaF
-
as efficient as Cl-, I-, NO2- or acetate, less efficient than citrate, phosphate or sulfate
NaI
-
as efficient as Cl-, F-, NO2- or acetate, less efficient than citrate, phosphate or sulfate
NaNO2
-
as efficient as Cl-, I-, F- or acetate, less efficient than citrate, phosphate or sulfate
phosphatidylinositol 4,5-bisphosphate
-
inhibits receptor phosphorylation, causes membrane association, 30% inhibition of phosphorylation of RRREEEEESAAA
propranolol
-
beta-adrenergic antagonist, in presence no phosphorylation
Protein kinase C inhibitor H7
-
quinpirole
-
inhibits GRK2 and GRK3
rhodopsin
-
intact light-activated rhodopsin slightly inhibits phosphorylation of RRREEEEESAAA
Sangivamycin
-
IC50: 0.067 mM
Sodium acetate
-
as efficient as Cl-, I-, NO2- or F-, less efficient than citrate, phosphate or sulfate
Sodium citrate
-
20 mM, 97% inhibition, more efficient than phosphate, sulfate, Cl-, F-, I-, NO2- or acetate
Sodium phosphate
-
20 mM, 76% inhibition, less efficient than citrate, as good as sulfate, more efficient than Cl-, F-, I-, NO2- or acetate
Sodium sulfate
-
less efficient than citrate, as good as phosphate, more efficient than Cl-, F-, I-, NO2- or acetate
spermidine
-
weak, less potent than polylysine
tamoxifen
-
IC50: 0.04 mM
Trifluoperazine
-
IC50: 0.035 mM
Triton X-100
-
IC50: 0.054 mM
Tween 20
-
IC50: 0.027 mM
Yohimbine
-
alpha2-adrenergic antagonist, co-incubation completely blocks phosphorylation of alpha2-adrenergic receptor
Zn2+
-
0.1-0.2 mM ZnCl2, 94-98% inhibition
2,3-diphosphoglycerate
-
weak
2,3-diphosphoglycerate
-
inhibits in the millimolar range, IC50: 1.1 mM with rhodopsin as substrate
Digitonin
-
IC50: 0.05 mM
Digitonin
-
0.05-0.1%, 93-95% inhibition
heparin
-
-
heparin
-
most potent inhibitor to date
heparin
-
strong, kinetics, IC50: 0.00003 mM with beta-AR as substrate, 0.00015 mM with rhodopsin as substrate
heparin
-
beta-ARK 1: IC50 is 0.0014 mM, beta-ARK 2: IC50 is 0.0011 mM
heparin
-
potent inhibitor of beta-ARK 1
heparin
-
0.001 mM, complete inhibition of muscarinic cholinergic receptor phosphorylation
heparin
-
polylysine, spermine or spermidine at lower concentrations partially reverses
heparin
-
de-N-sulfated heparin is 8fold less effective
heparin
-
inhibits both isozymes ARK1 and ARK2 potently with IC50 of 0.0014 mM and 0.0011 mM, respectively
Inositol hexasulfate
-
good inhibitor
Inositol hexasulfate
-
270fold more potent than inositol hexaphosphate
Inositol hexasulfate
-
IC50: 0.0135 mM with rhodopsin as substrate
NaCl
-
0.1 M, 90% inhibition
NaCl
-
20 mM, 48% inhibition, as efficient as F-, I-, NO2- or acetate, less efficient than citrate, phosphate or sulfate
peptide
-
synthetic peptides from a variety of intracellular regions of beta2-AR specifically inhibit phosphorylation of the intact receptor, but not of peptide substrates
peptide
-
synthetic peptides derived from the receptor intracellular loop inhibit
Polyaspartic acid
-
good inhibitor
Polyaspartic acid
-
IC50: 0.0013 mM with rhodopsin as substrate
Polyglutamic acid
-
good inhibitor
Polyglutamic acid
-
IC50: 0.002 mM with rhodopsin as substrate
polylysine
-
weak, more potent than spermine and spermidine
polylysine
-
IC50: 0.069 mM with rhodopsin as substrate
Protein kinase C inhibitor H7
-
weak
-
Protein kinase C inhibitor H7
-
IC50: 0.25 mM
-
pyridoxal 5'-phosphate
-
inhibits in the millimolar range
pyridoxal 5'-phosphate
-
weak, IC50: 0.9 mM with rhodopsin as substrate
spermine
-
IC50: 1.6 mM
spermine
-
weak, less potent than polylysine
additional information
-
-
-
additional information
-
marked inhibition of rhodopsin or synthetic peptide phosphorylation in the presence of increasing amounts of microsomal membranes, bound enzyme is less able to interact with its substrate
-
additional information
-
not affected by Ca2+ or Co2+
-
additional information
-
alprenolol is no inhibitor with alpha2-adrenergic receptor as substrate
-
additional information
-
platelet-derived growth factor receptor-beta activates the enzyme by tyrosine phosphorylation, the wild-type PDGFRbeta is 60fold more active with GRK2 than PDGFRbeta mutant Y857F, GRK2 activation also increases GRK2 degradation and downregulation
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Gbetagamma subunits
required for activity on G protein-coupled receptors, binding via enzyme C-terminal pleckstrin homology domain, binding does not induce large domain rearrangements, but small rotations of the enzyme domains, the domain interfaces remain intact upon GRK2 activation, structure analysis of GRK2 in complex with G protein beta1gamma2 subunits, overview
-
(-)-Epinephrine
-
requirement, agonist, alpha2-adrenergic receptor as substrate
AlF4-
-
enhances beta-ARK activity upon stimulation of heterotrimeric G proteins
alpha2A-adrenergic receptor
-
epinephrine-activated alpha2A-adrenergic receptor activates GRK2, interaction with GRK2 via the second and third intracellular loop of the receptor, determination of regions required for specific interaction utilizing recombinant GST-tagged wild-type and several mutant alpha2A ARs, residues R225, R226, R218, K320, R322, and K358 are important, overview
-
beta-arrestin2
-
mediates GRK activity, forms a signaling complex with filamin and dopamine D3 receptor, interactions, overview
-
beta2-adrenergic receptor
-
cAMP-dependent protein kinase
-
PKA-mediated phosphorylation favors subsequent phosphorylation of beta2-AR by beta-ARK, PKA increases the phosphorylation rate of beta-ARK
-
Carbachol
-
requirement, agonist, muscarinic cholinergic receptor as substrate
cardiolipin
-
activates, phosphorylation of beta2-AR
G protein betagamma-subunit
-
G protein Gbetagamma subunits
-
activate both ARK1 and ARK2 about 2.5fold
-
mastoparan/guanosine 5'-(3-O-thio)triphosphate
-
enhances beta-ARK activity upon stimulation of heterotrimeric G proteins
Oxytremorine
-
requirement, agonist, muscarinic cholinergic receptor as substrate
phosphatidic acid
-
activates, phosphorylation of beta2-AR
phosphatidylglycerol
-
activates, phosphorylation of beta2-AR
phosphatidylinositol
-
activates, phosphorylation of beta2-AR, 6fold activation of phosphorylation of RRREEEEESAAA
phosphatidylserine
-
activates, phosphorylation of beta2-AR
Phospholipid
-
required for phosphorylation of beta2-AR, activation is associated with a conformational change in beta-ARK 1, acidic phospholipid specificity, not activated by phosphatidylinositol 4,5-diphosphate, direct regulation of beta-ARK 1 activity by phospholipids
platelet-derived growth factor receptor-beta
-
activates the enzyme by tyrosine phosphorylation at Y13, Y86, and Y92, required, the wild-type PDGFRbeta is 60fold more active with GRK2 than PDGFRbeta mutant Y857F, GRK2 activation also increases GRK2 degradation and downregulation, independent of Gbetagamma subunits and phosphoinositide 3-kinase
-
rhodopsin
-
interaction of enzyme with light-activated rhodopsin or truncated rhodopsin lacking its C-terminal phosphorylation sites activates peptide phosphorylation, at lower concentrations, enhances both the affinity and catalytic efficiency for peptide phosphorylation, but intact light-activated rhodopsin slightly inhibits the phosphorylation of RRREEEEESAAA
beta2-adrenergic receptor
-
interaction of enzyme with human agonist-occupied receptor specifically and significantly enhances peptide phosphorylation, at lower concentrations, enhances both the affinity and catalytic efficiency for peptide phosphorylation
-
beta2-adrenergic receptor
-
interaction of beta-ARK 1 with the agonist-occupied receptor activates
-
G protein
-
GRK2 binds G protein beta1gamma2 subunits, binding structure, no correct complex formation with recombinant Gbetagamma mutant C68S lacking the isoprenylation site, overview
-
G protein
-
GRK2 binds G protein beta1gamma2 subunits, binding structure, overview
-
G protein
-
required for GRK2 activation
-
G protein betagamma-subunit
-
-
-
G protein betagamma-subunit
-
activates, binding domain is localized to the C-terminal region of beta-ARK
-
G protein betagamma-subunit
-
from brain, binds to the C-terminal half of the PH domain
-
G protein betagamma-subunit
-
from bovine brain, beta-ARK 1 and 2: requirement, selectivity for betagamma subunits, both isoforms differentiate between defined betagamma subunits
-
G protein betagamma-subunit
-
10fold activation, beta-ARK 1 and 2, increases incorporation of phosphate from 4 to 10 mol phosphate/mol receptor
-
G protein betagamma-subunit
-
requirement, binding plays an important role in specifically targeting the enzyme complex to its receptor substrate
-
isoproterenol
-
stimulates
isoproterenol
-
requirement, beta-agonist, beta-adrenergic receptor as substrate
isoproterenol
requirement, beta-agonist, beta-adrenergic receptor as substrate
isoproterenol
-
requirement, beta-agonist, beta-adrenergic receptor as substrate
additional information
-
partial agonists promote reduced receptor phosphorylation
-
additional information
-
not effected by Ca2+ or Co2+
-
additional information
-
not activated by polycations
-
additional information
-
alpha2-AR phosphorylation is not stimulated by isoproterenol
-
additional information
-
agonists induce specific conformational changes allowing phosphorylation
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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0.0012
4-(3-((2,6-bis(trifluoromethyl)benzyl)carbamoyl)-4-fluorophenyl)-N-(1H-indazol-5-yl)-6-methyl-2-oxo-1,2,3,4-tetrahydropyrimidine-5-carboxamide
Bos taurus
at pH 7.0, temperature not specified in the publication
0.00013
4-(3-((2,6-dichlorobenzyl)carbamoyl)-4-fluorophenyl)-N-(1H-indazol-5-yl)-6-methyl-2-oxo-1,2,3,4-tetrahydropyrimidine-5-carboxamide
Bos taurus
at pH 7.0, temperature not specified in the publication
0.00022
4-(3-((2,6-difluorobenzyl)carbamoyl)-4-fluorophenyl)-N-(1H-indazol-5-yl)-6-methyl-2-oxo-1,2,3,4-tetrahydropyrimidine-5-carboxamide
Bos taurus
at pH 7.0, temperature not specified in the publication
0.00013
4-(3-((2,6-dimethoxybenzyl)carbamoyl)-4-fluorophenyl)-N-(1Hindazol-5-yl)-6-methyl-2-oxo-1,2,3,4-tetrahydropyrimidine-5-carboxamide
Bos taurus
at pH 7.0, temperature not specified in the publication
0.00007
4-(3-((2,6-dimethylbenzyl)carbamoyl)-4-fluorophenyl)-N-(1H-indazol-5-yl)-6-methyl-2-oxo-1,2,3,4-tetrahydropyrimidine-5 carboxamide
Bos taurus
at pH 7.0, temperature not specified in the publication
0.0046
4-(3-((2,6-dimethylbenzyl)carbamoyl)-4-fluorophenyl)-N-(1H-indazol-5-yl)-N,6-dimethyl-2-oxo-1,2,3,4-tetrahydropyrimidine-5-carboxamide
Bos taurus
at pH 7.0, temperature not specified in the publication
0.00023
4-(3-((2,6-dimethylphenethyl)carbamoyl)-4-fluorophenyl)-N-(1H-indazol-5-yl)-6-methyl-2-oxo-1,2,3,4-tetrahydropyrimidine-5-carboxamide
Bos taurus
at pH 7.0, temperature not specified in the publication
0.0027
4-(3-((3,5-bis(trifluoromethyl)benzyl)carbamoyl)-4-fluorophenyl)-N-(1H-indazol-5-yl)-6-methyl-2-oxo-1,2,3,4-tetrahydropyrimidine-5-carboxamide
Bos taurus
at pH 7.0, temperature not specified in the publication
0.1
4-(3-(2-((2,6-bis(trifluoromethyl)benzyl)amino)-2-oxoethyl)-4-fluorophenyl)-N-(1H-indazol-5-yl)-6-methyl-2-oxo-1,2,3,4-tetrahydropyrimidine-5-carboxamide
Bos taurus
at pH 7.0, temperature not specified in the publication
0.00045
4-(3-(2-((2,6-dimethoxybenzyl)amino)-2-oxoethyl)-4-fluorophenyl)-N-(1H-indazol-5-yl)-6-methyl-2-oxo-1,2,3,4-tetrahydropyrimidine-5-carboxamide
Bos taurus
at pH 7.0, temperature not specified in the publication
0.025
4-(3-(2-((2,6-dimethylbenzyl)amino)-2-oxoethyl)-4-fluorophenyl)-N-(1H-indazol-5-yl)-6-methyl-2-oxo-1,2,3,4-tetrahydropyrimidine-5-carboxamide
Bos taurus
at pH 7.0, temperature not specified in the publication
0.00069
4-(3-(benzylcarbamoyl)-4-fluorophenyl)-N-(1H-indazol-5-yl)-6-methyl-2-oxo-1,2,3,4-tetrahydropyrimidine-5-carboxamide
Bos taurus
at pH 7.0, temperature not specified in the publication
0.0019
4-(4-fluoro-3-(((3-methylpyridin-2-yl)methyl)carbamoyl)phenyl)-N-(1H-indazol-5-yl)-6-methyl-2-oxo-1,2,3,4-tetrahydropyrimidine-5-carboxamide
Bos taurus
at pH 7.0, temperature not specified in the publication
0.00028
4-(4-fluoro-3-((2-(pyridin-2-yl)ethyl)carbamoyl)phenyl)-N-(1H-indazol-5-yl)-6-methyl-2-oxo-1,2,3,4-tetrahydropyrimidine-5-carboxamide
Bos taurus
at pH 7.0, temperature not specified in the publication
0.0048
4-(4-fluoro-3-((2-(pyridin-4-yl)ethyl)carbamoyl)phenyl)-N-(1H-indazol-5-yl)-6-methyl-2-oxo-1,2,3,4-tetrahydropyrimidine-5-carboxamide
Bos taurus
at pH 7.0, temperature not specified in the publication
0.00006
4-(4-fluoro-3-((2-methoxybenzyl)carbamoyl)phenyl)-N-(1H-indazol-5-yl)-6-methyl-2-oxo-1,2,3,4-tetrahydropyrimidine-5-carboxamide
Bos taurus
at pH 7.0, temperature not specified in the publication
0.0002
4-(4-fluoro-3-((3-fluorobenzyl)carbamoyl)phenyl)-N-(1H-indazol-5-yl)-6-methyl-2-oxo-1,2,3,4-tetrahydropyrimidine-5-carboxamide
Bos taurus
at pH 7.0, temperature not specified in the publication
0.00042
4-(4-fluoro-3-((3-methoxybenzyl)carbamoyl)phenyl)-N-(1H-indazol-5-yl)-6-methyl-2-oxo-1,2,3,4-tetrahydropyrimidine-5-carboxamide
Bos taurus
at pH 7.0, temperature not specified in the publication
0.00046
4-(4-fluoro-3-((4-methoxybenzyl)carbamoyl)phenyl)-N-(1H-indazol-5-yl)-6-methyl-2-oxo-1,2,3,4-tetrahydropyrimidine-5-carboxamide
Bos taurus
at pH 7.0, temperature not specified in the publication
0.00028
4-(4-fluoro-3-((isoquinolin-1-ylmethyl)carbamoyl)phenyl)-N-(1H-indazol-5-yl)-6-methyl-2-oxo-1,2,3,4-tetrahydropyrimidine-5-carboxamide
Bos taurus
at pH 7.0, temperature not specified in the publication
0.00015
4-(4-fluoro-3-((pyridin-2-ylmethyl)carbamoyl)phenyl)-N-(1H-indazol-5-yl)-6-methyl-2-oxo-1,2,3,4-tetrahydropyrimidine-5-carboxamide
Bos taurus
at pH 7.0, temperature not specified in the publication
0.0043
4-(4-fluoro-3-(methylcarbamoyl)phenyl)-N-(1H-indazol-5-yl)-6-methyl-2-oxo-1,2,3,4-tetrahydropyrimidine-5-carboxamide
Bos taurus
at pH 7.0, temperature not specified in the publication
0.02
5-(5-((1H-indazol-5-yl)carbamoyl)-6-methyl-2-oxo-1,2,3,4-tetrahydropyrimidin-4-yl)-2-fluorobenzoic acid
Bos taurus
at pH 7.0, temperature not specified in the publication
0.00013
CCG-224406
Bos taurus
at pH 7.0, temperature not specified in the publication
0.00077
GSK180736A
Bos taurus
at pH 7.0, temperature not specified in the publication
0.1
N-(benzo[d][1,3]dioxol-5-yl)-4-(4-fluoro-3-((pyridin-2-ylmethyl)-carbamoyl)phenyl)-6-methyl-2-oxo-1,2,3,4-tetrahydropyrimidine-5-carboxamide
Bos taurus
at pH 7.0, temperature not specified in the publication
0.00138
paroxetine
Bos taurus
at pH 7.0, temperature not specified in the publication
0.00002
Takeda103A
Bos taurus
at pH 7.0, temperature not specified in the publication
1.1
2,3-diphosphoglycerate
Bos taurus
-
inhibits in the millimolar range, IC50: 1.1 mM with rhodopsin as substrate
0.043
Chloropromazine
Bos taurus
-
IC50: 0.043 mM
7.3
D-glucosamine 2,6-disulfate
Bos taurus
-
inhibits in the millimolar range, weak, IC50: 7.3 mM with rhodopsin as substrate
0.027
D-sphingosine
Bos taurus
-
IC50: 0.027 mM
0.00015
Dextran sulfate
Bos taurus
-
strong, IC50: 0.00015 mM with rhodopsin as substrate
-
0.05
Digitonin
Bos taurus
-
IC50: 0.05 mM
3.6
Inositol hexaphosphate
Bos taurus
-
weak, IC50: 3.6 mM with rhodopsin as substrate
0.0135
Inositol hexasulfate
Bos taurus
-
IC50: 0.0135 mM with rhodopsin as substrate
0.0013
Polyaspartic acid
Bos taurus
-
IC50: 0.0013 mM with rhodopsin as substrate
0.002
Polyglutamic acid
Bos taurus
-
IC50: 0.002 mM with rhodopsin as substrate
0.069
polylysine
Bos taurus
-
IC50: 0.069 mM with rhodopsin as substrate
0.25
Protein kinase C inhibitor H7
Bos taurus
-
IC50: 0.25 mM
-
0.9
pyridoxal 5'-phosphate
Bos taurus
-
weak, IC50: 0.9 mM with rhodopsin as substrate
0.067
Sangivamycin
Bos taurus
-
IC50: 0.067 mM
1.6
spermine
Bos taurus
-
IC50: 1.6 mM
0.04
tamoxifen
Bos taurus
-
IC50: 0.04 mM
0.035
Trifluoperazine
Bos taurus
-
IC50: 0.035 mM
0.054
Triton X-100
Bos taurus
-
IC50: 0.054 mM
0.027
Tween 20
Bos taurus
-
IC50: 0.027 mM
0.00003
heparin
Bos taurus
-
strong, kinetics, IC50: 0.00003 mM with beta-AR as substrate, 0.00015 mM with rhodopsin as substrate
0.0011
heparin
Bos taurus
-
beta-ARK 1: IC50 is 0.0014 mM, beta-ARK 2: IC50 is 0.0011 mM
0.0014
heparin
Bos taurus
-
inhibits both isozymes ARK1 and ARK2 potently with IC50 of 0.0014 mM and 0.0011 mM, respectively
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E520A
site-directed mutagenesis, very low recombinant expression level, mutant GRK2 shows a dramatic loss of activity with rhodopsin as substrate
E96A
site-directed mutagenesis, slightly increased recombinant expression level compared to the wild-type GRK2, mutant GRK2 shows activity with rhodopsin as substrate similar to the wild-type enzyme
P638D
site-directed mutagenesis, RH-PH domain interface residue mutant, 40% reduced recombinant expression level compared to the wild-type GRK2, mutant GRK2 shows 15% of wild-type activity with rhodopsin as substrate
R516A
site-directed mutagenesis, 60% reduced recombinant expression level compared to the wild-type GRK2, mutant GRK2 shows slightly reduced activity with rhodopsin as substrate
S670A
site-directed mutagenesis, the MAP kinase phosphorylation site S670 is eliminated in the GRK2 mutant enzyme
V42E
site-directed mutagenesis, RH-PH domain interface residue mutant, 60% reduced recombinant expression level compared to the wild-type GRK2, mutant GRK2 shows 25% of wild-type activity with rhodopsin as substrate
Y46A
site-directed mutagenesis, RH-PH domain interface residue mutant, 80% reduced recombinant expression level compared to the wild-type GRK2, mutant GRK2 shows 50% of wild-type activity with rhodopsin as substrate
C221V
-
site-directed mutagenesis, mutant GRK2 activity is slightly increased compared to the wild-type enzyme, the requirement for initial ligand-induced internalization of a G protein-coupled receptor with subsequent rounds of internalization is different for the mutant GRK2 compared to the wild-type enzyme
D110A/K220R
-
double mutant has a disrupted RGS (regulator of G protein signalling) function. Although double mutant coimmunoprecipitates with the histamine H2 receptor, it reverses GRK2K220R-mediated histamine H2 receptor desensitization
D635K/S636K/D637K
-
triple mutant D635K/S636K/D637K, mutation in the Gbetagamma-binding region of the PH domain
D637K
-
triple mutant D635K/S636K/D637K, mutation in the Gbetagamma-binding region of the PH domain
DELTA495-689
-
carboxyl-terminus is expressed as a Flag-tagged betaARKct (GRK2 amino acids 495-689) in HeLa and HEK293 cells
E646K
-
mutation in the Gbetagamma-binding region of the PH domain
K567E
-
mutation in the PIP2-binding region of the PH domain
K645E
-
mutation in the Gbetagamma-binding region of the PH domain
L271G
-
site-directed mutagenesis, mutant GRK2 shows highly reduced activity compared to the wild-type enzyme
L273Y
-
site-directed mutagenesis, mutant GRK2 shows highly reduced activity compared to the wild-type enzyme
L336F
-
site-directed mutagenesis, mutant GRK2 shows highly reduced activity compared to the wild-type enzyme
L647G
-
residue of the PH domain, mutation completely abolishes beta-ARK activity and activation by the G protein betagamma-subunit
Q642G
-
mutation in the Gbetagamma-binding region of the PH domain
R578N
-
double mutant R578N/R579N, mutation in the PIP2-binding region of the PH domain
R579N
-
double mutant R578N/R579N, mutation in the PIP2-binding region of the PH domain
S636K
-
triple mutant D635K/S636K/D637K, mutation in the Gbetagamma-binding region of the PH domain
S670A
-
cells overexpressing the S670A-GRK2 mutant have less H2O2-induced death as determined by the terminal deoxynucleotidyl transferase dUTP nick end labeling assay. In cells expressing mutant GRK2, the amount of cell death is significantly reduced by 36.4%. Mutant displays significantly less Hsp90 binding in myocytes after oxidative stress compared with wild-type GRK2. Nonphosphorylated mutant S670A is not localized to mitochondria after oxidative stress
S670D
-
mutant shows the highest level of interaction with Hsp90 compared to wild-type and mutant S670A
W576A
-
mutation in the PIP2-binding region of the PH domain
W643A
-
residue of the PH domain, mutation completely abolishes beta-ARK activity and activation by the G protein betagamma-subunit
Y13F
-
site-directed mutagenesis, required activating tyrosine phosphorylation by platelet-derived growth factor receptor-beta kinase activity is reduced with the mutant GRK2, reduced activity compared to the wild-type
Y13F/Y86F/Y92F
-
site-directed mutagenesis, required activating tyrosine phosphorylation by platelet-derived growth factor receptor-beta kinase activity is eliminated with the mutant GRK2, reduced activity compared to the wild-type
Y86F
-
site-directed mutagenesis, required activating tyrosine phosphorylation by platelet-derived growth factor receptor-beta kinase activity is reduced with the mutant GRK2, reduced activity compared to the wild-type
Y86F/Y92F
-
site-directed mutagenesis, required activating tyrosine phosphorylation by platelet-derived growth factor receptor-beta kinase activity is highly reduced with the mutant GRK2, reduced activity compared to the wild-type
Y92F
-
site-directed mutagenesis, required activating tyrosine phosphorylation by platelet-derived growth factor receptor-beta kinase activity is reduced with the mutant GRK2, reduced activity compared to the wild-type
D110A
-
the mutant shows impaired binding to Galphaq proteins, mutant GRK2 inhibits ERK phosphorylation similar to the wild-type enzyme when co-expressed with CCR2B in HEK-293 cells
D110A
-
the expression of the D110A mutant in COS7-transfected cells fails to desensitize the histamine H2 receptor
K220R
-
mutant GRK2 inhibits ERK phosphorylation in a slightly reduced rate compared to the wild-type enzyme when co-expressed with CCR2B in HEK-293 cells
K220R
-
inactive GRK2 mutant
K220R
-
catalytically inactive mutant. Mutant cells desensitize histamine H2 receptor signaling in the same degree as the GRK2 wild type cells. Although the receptor phosphorylation is crucial for histamine H2 receptor internalization and resensitization, the kinase activity is not required to achieve histamine H2 receptor desensitization
additional information
-
effects of mutations in the pleckstrin homology domain of beta-ARK on activity, Ala-insertion following Trp-643 completely abolishes beta-ARK activity and activation by the G protein betagamma-subunit
additional information
-
adenovirus-mediated expression of beta-adrenergic receptor kinase C-terminus reduces intimal hyperplasia and luminal stenosis of arteriovenous polytetrafluoroethylene grafts in pigs
additional information
-
construction of a deletion GRK2 mutant comprising residues 438-689, which does not inhibit ERK phosphorylation when co-expressed with CCR2B in HEK-293 cells
additional information
-
targeted tissue-specific overexpression of GRK2 in mouse osteoblasts attenuates parathyroid hormone receptor PTH signaling, and promotes bone loss with decreased osteoclastic activity and decreased osteoblasts and trabecular bone, equal effects in female and male mice, overview
additional information
-
transient overexpression of wild-type GRK2 in NG108-15 mouse neuroblastoma x rat glioma hybrid cells leads to selective inhibition of A2 adenosine receptor responsiveness, but does not affect secretin-stimulated cyclic AMP accumulation
additional information
-
knockdown of endogenous GRK2 by short hairpin RNA significantly reduces signaling in response to the Smoothened agonist SAG and also inhibits signaling induced by an oncogenic Smoothened mutant, Smo M2
additional information
-
to identify the domains responsible for the kinase-independent receptor desensitization, the histamine H2 receptor is co-transfected with constructions encoding the GRK2 RGS-homology domain (RH) and the RH or the kinase domain fused to the pleckstrin homology domain. Results demonstrate that the RH domain of GRK2 is sufficient to desensitize the histamine H2 receptor
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Benovic, J.L.
Purification and characterization of beta-adrenergic receptor kinase
Methods Enzymol.
200
351-362
1991
Bos taurus
brenda
Benovic, J.L.; DeBlasi, A.; Stone, W.C.; Caron, M.G.; Lefkowitz, R.J.
Beta-adrenergic receptor kinase: primary structure delineates a multigene family
Science
246
235-240
1989
Bos taurus, Bos taurus (P21146)
brenda
Chuang, T.T.; Sallese, M.; Ambrosini, G.; Parruti, G.; De Blasi, A.
High expression of beta-adrenergic receptor kinase in human peripheral blood leukocytes. Isoproterenol and platelet activating factor can induce kinase translocation
J. Biol. Chem.
267
6886-6892
1992
Bos taurus, Homo sapiens, Homo sapiens (P25098)
brenda
Benovic, J.L.; Onorato, J.J.; Arriza, J.L.; Stone, W.C.; Lohse, M.; Jenkins, N.A.; Gilbert, D.J.; Copeland, N.G.; Caron, M.G.; Lefkowitz, R.J.
Cloning, expression, and chromosomal localization of beta-adrenergic receptor kinase 2. A new member of the receptor kinase family
J. Biol. Chem.
266
14939-14946
1991
Bos taurus (P26818), Bos taurus
brenda
Parruti, G.; Ambrosini, G.; Sallese, M.; De Blasi, A.
Molecular cloning, functional expression and mRNA analysis of human beta-adrenergic receptor kinase 2
Biochem. Biophys. Res. Commun.
190
475-481
1993
Bos taurus, Homo sapiens (P35626), Homo sapiens
brenda
Benovic, J.L.; Mayor, F.; Somers, R.L.; Caron, M.G.; Lefkowitz, R.J.
Light-dependent phosphorylation of rhodopsin by beta-adrenergic receptor kinase
Nature
321
869-872
1986
Bos taurus
brenda
Onorato, J.J.; Palczewski, K.; Regan, J.W.; Caron, M.G.; Lefkowitz, R.J.; Benovic, J.L.
Role of acidic amino acids in peptide substrates of the beta-adrenergic receptor kinase and rhodopsin kinase
Biochemistry
30
5118-5125
1991
Bos taurus
brenda
Benovic, J.L.; Regan, J.W.; Matsui, H.; Mayor, F.; Cotecchia, S.; Leeb-Lundberg, L.M.F.; Caron, M.G.; Lefkowitz, R.J.
Agonist-dependent phosphorylation of the alpha 2-adrenergic receptor by the beta-adrenergic receptor kinase
J. Biol. Chem.
262
17251-17253
1987
Bos taurus
brenda
Benovic, J.L.; Mayor, F.; Staniczewski, C.; Lefkowitz, R.J.; Caron, M.G.
Purification and characterization of the beta-adrenergic receptor kinase
J. Biol. Chem.
262
9026-9032
1987
Bos taurus
brenda
Benovic, J.L.; Stone, W.C.; Caron, M.G.; Lefkowitz, R.J.
Inhibition of the beta-adrenergic receptor kinase by polyanions
J. Biol. Chem.
264
6707-6710
1989
Bos taurus
brenda
Kwatra, M.M.; Benovic, J.L.; Caron, M.G.; Lefkowitz, R.J.; Hosey, M.M.
Phosphorylation of chick heart muscarinic cholinergic receptors by the beta-adrenergic receptor kinase
Biochemistry
28
4543-4547
1989
Bos taurus
brenda
Shlemann, P.; Hekman, M.; Buchen, C.; Elce, J.S.; Lohse, M.J.
Purification and functional characterization of beta-adrenergic receptor kinase expressed in insect cells
FEBS Lett.
324
59-62
1993
Bos taurus, Homo sapiens
brenda
Kim, C.M.; Dion, S.B.; Onorato, J.J.; Benovic, J.L.
Expression and characterization of two beta-adrenergic receptor kinase isoforms using the baculovirus expression system
Receptor
3
39-55
1993
Bos taurus
brenda
Chen, C.Y.; Dion, S.B.; Kim, C.M.; Benovic, J.L.
Beta-adrenergic receptor kinase. Agonist-dependent receptor binding promotes kinase activation
J. Biol. Chem.
268
7825-7831
1993
Bos taurus
brenda
Goldman, P.S.; DeMaggio, A.J.; Hoekstra, M.F.; Goodman, R.H.
The beta-adrenergic receptor kinase interacts with the amino terminus of the G protein beta subunit
Biochem. Biophys. Res. Commun.
240
425-429
1997
Bos taurus
brenda
Touhara, K.
Effects of mutations in pleckstrin homology domain on beta-adrenergic receptor kinase activity in intact cells
Biochem. Biophys. Res. Commun.
252
669-674
1998
Bos taurus
brenda
Moffett, S.; Rousseau, G.; Lagace, M.; Bouvier, M.
The palmitoylation state of the beta2-adrenergic receptor regulates the synergistic action of cyclic AMP-dependent protein kinase and beta-adrenergic receptor kinase involved in its phosphorylation and desensitization
J. Neurochem.
76
269-279
2001
Bos taurus
brenda
Murga, C.; Esteban, N.; Ruiz-Gomez, A.; Mayor, F.Jr.
The basal subcellular distribution of beta-adrenergic receptor kinase is independent of G-protein betagamma subunits
FEBS Lett.
409
24-28
1997
Bos taurus
brenda
Mller, S.; Straub, A.; Lohse, M.J.
Selectivity of beta-adrenergic receptor kinase 2 for G protein betagamma subunits
FEBS Lett.
401
25-29
1997
Bos taurus
brenda
Touhara, K.
Binding of multiple ligands to pleckstrin homology domain regulates membrane translocation and enzyme activity of beta-adrenergic receptor kinase
FEBS Lett.
417
243-248
1997
Bos taurus
brenda
Murga, C.; Ruiz-Gomez, A.; Garcia-Higuera, I.; Kim, C.M.; Benovic, J.L.; Mayor, F.Jr.
High affinity binding of beta-adrenergic receptor kinase to microsomal membranes. Modulation of the activity of bound kinase by heterotrimeric G protein activation
J. Biol. Chem.
271
985-994
1996
Bos taurus
brenda
Onorato, J.J.; Gillis, M.E.; Liu, Y.; Benovic, J.L.; Ruoho, A.E.
The beta-adrenergic receptor kinase (GRK2) is regulated by phospholipids
J. Biol. Chem.
270
21346-21353
1995
Bos taurus
brenda
Lodowski, D.T.; Barnhill, J.F.; Pitcher, J.A.; Capel, W.D.; Lefkowitz, R.J.; Tesmer, J.J.
Purification, crystallization and preliminary X-ray diffraction studies of a complex between G protein-coupled receptor kinase 2 and Gbeta1gamma2
Acta Crystallogr. Sect. D
59
936-939
2003
Bos taurus
brenda
Wang, L.; Liu, S.; Quarles, L.D.; Spurney, R.F.
Targeted overexpression of G protein-coupled receptor kinase-2 in osteoblasts promotes bone loss
Am. J. Physiol.
288
E826-834
2005
Bos taurus
brenda
Lodowski, D.T.; Barnhill, J.F.; Pyskadlo, R.M.; Ghirlando, R.; Sterne-Marr, R.; Tesmer, J.J.
The role of Gbetagamma and domain interfaces in the activation of G protein-coupled receptor kinase 2
Biochemistry
44
6958-6970
2005
Bos taurus (P21146)
brenda
Ghadessy, R.S.; Willets, J.M.; Kelly, E.
G protein-coupled receptor kinase 6 (GRK6) selectively regulates endogenous secretin receptor responsiveness in NG108-15 cells
Br. J. Pharmacol.
138
660-670
2003
Bos taurus
brenda
Luo, Z.; Akita, G.Y.; Date, T.; Treleaven, C.; Vincent, K.A.; Woodcock, D.; Cheng, S.H.; Gregory, R.J.; Jiang, C.
Adenovirus-mediated expression of beta-adrenergic receptor kinase C-terminus reduces intimal hyperplasia and luminal stenosis of arteriovenous polytetrafluoroethylene grafts in pigs
Circulation
111
1679-1684
2005
Bos taurus
brenda
Pao, C.S.; Benovic, J.L.
Structure/function analysis of alpha2A-adrenergic receptor interaction with G protein-coupled receptor kinase 2
J. Biol. Chem.
280
11052-11058
2005
Bos taurus
brenda
Kim, K.M.; Gainetdinov, R.R.; Laporte, S.A.; Caron, M.G.; Barak, L.S.
G protein-coupled receptor kinase regulates dopamine D3 receptor signaling by modulating the stability of a receptor-filamin-beta-arrestin complex. A case of autoreceptor regulation
J. Biol. Chem.
280
12774-12780
2005
Bos taurus
brenda
Wu, J.H.; Goswami, R.; Kim, L.K.; Miller, W.E.; Peppel, K.; Freedman, N.J.
The platelet-derived growth factor receptor-beta phosphorylates and activates G protein-coupled receptor kinase-2. A mechanism for feedback inhibition
J. Biol. Chem.
280
31027-31035
2005
Bos taurus
brenda
Kenski, D.M.; Zhang, C.; von Zastrow, M.; Shokat, K.M.
Chemical genetic engineering of G protein-coupled receptor kinase 2
J. Biol. Chem.
280
35051-35061
2005
Bos taurus
brenda
Jimenez-Sainz, M.C.; Murga, C.; Kavelaars, A.; Jurado-Pueyo, M.; Krakstad, B.F.; Heijnen, C.J.; Mayor, F.Jr.; Aragay, A.M.
G protein-coupled receptor kinase 2 negatively regulates chemokine signaling at a level downstream from G protein subunits
Mol. Biol. Cell
17
25-31
2006
Bos taurus, Mus musculus
brenda
Lodowski, D.T.; Pitcher, J.A.; Capel, W.D.; Lefkowitz, R.J.; Tesmer, J.J.
Keeping G proteins at bay: a complex between G protein-coupled receptor kinase 2 and Gbetagamma
Science
300
1256-1262
2003
Bos taurus
brenda
Meloni, A.R.; Fralish, G.B.; Kelly, P.; Salahpour, A.; Chen, J.K.; Wechsler-Reya, R.J.; Lefkowitz, R.J.; Caron, M.G.
Smoothened signal transduction is promoted by G protein-coupled receptor kinase 2
Mol. Cell. Biol.
26
7550-7560
2006
Bos taurus
brenda
Chen, M.; Sato, P.Y.; Chuprun, J.K.; Peroutka, R.J.; Otis, N.J.; Ibetti, J.; Pan, S.; Sheu, S.S.; Gao, E.; Koch, W.J.
Prodeath signaling of g protein-coupled receptor kinase 2 in cardiac myocytes after ischemic stress occurs via extracellular signal-regulated kinase-dependent heat shock protein 90-mediated mitochondrial targeting
Circ. Res.
112
1121-1134
2013
Bos taurus, Rattus norvegicus
brenda
Fernandez, N.; Gottardo, F.L.; Alonso, M.N.; Monczor, F.; Shayo, C.; Davio, C.
Roles of phosphorylation-dependent and -independent mechanisms in the regulation of histamine H2 receptor by G protein-coupled receptor kinase 2
J. Biol. Chem.
286
28697-28706
2011
Bos taurus
brenda
Waldschmidt, H.V.; Homan, K.T.; Cruz-Rodriguez, O.; Cato, M.C.; Waninger-Saroni, J.; Larimore, K.M.; Cannavo, A.; Song, J.; Cheung, J.Y.; Kirchhoff, P.D.; Koch, W.J.; Tesmer, J.J.; Larsen, S.D.
Structure-based design, synthesis, and biological evaluation of highly selective and potent G protein-coupled receptor kinase 2 inhibitors
J. Med. Chem.
59
3793-3807
2016
Bos taurus (P21146)
brenda