2.7.11.15 (-)-Epinephrine requirement, agonist, alpha2-adrenergic receptor as substrate 645000 2.7.11.15 AlF4- enhances beta-ARK activity upon stimulation of heterotrimeric G proteins 645026 2.7.11.15 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 662332 2.7.11.15 arrestins arrestins modulate the enzyme activity having a regulatory role, regulation of arrestins, overview 662911 2.7.11.15 beta-arrestin required for phosphorylation activity and receptor substrate endocytosis 662153 2.7.11.15 beta-arrestin-2 forms a complex with GRK3 causing G protein-coupled receptor desensitization 662131 2.7.11.15 beta-arrestin-2 required, membrane protein 661684 2.7.11.15 beta-arrestin2 mediates GRK activity, forms a signaling complex with filamin and dopamine D3 receptor, interactions, overview 662345 2.7.11.15 beta2-adrenergic receptor interaction of beta-ARK 1 with the agonist-occupied receptor activates 645028 2.7.11.15 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 645012 2.7.11.15 cAMP-dependent protein kinase PKA-mediated phosphorylation favors subsequent phosphorylation of beta2-AR by beta-ARK, PKA increases the phosphorylation rate of beta-ARK 645020 2.7.11.15 Carbachol requirement, agonist, muscarinic cholinergic receptor as substrate 645005 2.7.11.15 cardiolipin activates, phosphorylation of beta2-AR 645028 2.7.11.15 corticotropin-releasing factor induces GRK2 expression in pituitary cells, suppressed by astressin, opposite effect compared to pituitary cells 661606 2.7.11.15 G protein binding and modulation of GRK2 and GRK3, Gbetagamma subunits bind GRK2 required for lipid association and G protein-coupled receptor phosphorylation and are released afterwards 661455 2.7.11.15 G protein binding of Gbeta/gamma dimers, activation is required for translocation from cytosol to plasma membrane 662911 2.7.11.15 G protein GRK2 binds G protein beta1gamma2 subunits, binding structure, no correct complex formation with recombinant Gbetagamma mutant C68S lacking the isoprenylation site, overview 660579 2.7.11.15 G protein GRK2 binds G protein beta1gamma2 subunits, binding structure, overview 663391 2.7.11.15 G protein interaction via GRK2 N-terminal RGS domain, binding of free Gbetagamma subunits initiates GRK2 translocation from cytosol to the plasma membrane and its activation for receptor phosphorylation 662767 2.7.11.15 G protein required for GRK2 activation 662818 2.7.11.15 G protein betagamma-subunit - 645028 2.7.11.15 G protein betagamma-subunit 10fold activation, beta-ARK 1 and 2, increases incorporation of phosphate from 4 to 10 mol phosphate/mol receptor 645011 2.7.11.15 G protein betagamma-subunit activates, binding domain is localized to the C-terminal region of beta-ARK 645013, 645015, 645026 2.7.11.15 G protein betagamma-subunit from bovine brain, beta-ARK 1 and 2: requirement, selectivity for betagamma subunits, both isoforms differentiate between defined betagamma subunits 645022 2.7.11.15 G protein betagamma-subunit from brain, binds to the C-terminal half of the PH domain 645015 2.7.11.15 G protein betagamma-subunit from brain, stimulates the phosphorylation of rhodopsin, but not of the peptide RRREEEEESAAA, an intact N-terminus of the gamma subunit is required for stimulation, but not for kinase binding, endoprotease Lys-C blocks stimulation, Gbetagamma binds to the C-terminal region of beta-ARK containing the pleckstrin homology domain, role of the G protein gamma-subunit 645025 2.7.11.15 G protein betagamma-subunit required for maximum activity, targets beta-ARK 1 to the membrane, which presumably facilitates the precise orchestration of phosphorylation of only activated receptors 645027 2.7.11.15 G protein betagamma-subunit requirement, binding plays an important role in specifically targeting the enzyme complex to its receptor substrate 645023 2.7.11.15 G protein Gbetagamma subunits activate both ARK1 and ARK2 about 2.5fold 645011 2.7.11.15 G protein Gbetagamma subunits required for activity, 20fold stimulation with substrate rhodopsin, 2 regulatory Gbetagamma binding sites: one N-terminal domain of GRK2, and one C-terminal within the pleckstrin homology domain, both sites are functionally different, overview 662179 2.7.11.15 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 661202 2.7.11.15 Insulin initiates GRK2 membrane translocation 674831 2.7.11.15 Insulin leads to increase dopamine D1 receptor serine phosphorylation by GRK2 671267 2.7.11.15 isoproterenol requirement, beta-agonist, beta-adrenergic receptor as substrate 490911, 490985, 490989, 640698, 640709, 644999, 645000, 645001, 645003, 645005 2.7.11.15 isoproterenol stimulates 645028 2.7.11.15 mastoparan/guanosine 5'-(3-O-thio)triphosphate enhances beta-ARK activity upon stimulation of heterotrimeric G proteins 645026 2.7.11.15 additional information activation of Toll-like receptors significantly increases GRK2 expression in primary macrophages, mechanism, overview 689035 2.7.11.15 additional information agonists induce specific conformational changes allowing phosphorylation 645005 2.7.11.15 additional information alpha2-AR phosphorylation is not stimulated by isoproterenol 645000 2.7.11.15 additional information autoregulation by a pseudosubstrate mechanism, overview 490797 2.7.11.15 additional information GRK2 is activated by phosphorylation through c-Src in a positive feedback reaction, Hsp90 secures proper folding and maturation and protects GRK2 from ubiquitination and proteasomal degradation, it induces GRK2 expression, phosphoinositol kinase 3 binds GRK2 and enhances receptor internalization 677232 2.7.11.15 additional information GRK2 is activated by phosphorylation through kinases c-SRC, PKA and PKC, and it is activated by phospholipids 672408 2.7.11.15 additional information GRK3 bind the Gbetagamma subunit complex, a process that induces activation of the GRKs by phosphorylation 677258 2.7.11.15 additional information myocardial ischemia: beta-ARK is activated, rapid induction of beta-ARK 1 activity in membranes, presumably caused by the release of the receptor agonist noradrenaline 645024 2.7.11.15 additional information not activated by cAMP, cGMP, Ca2+/calmodulin, Ca2+/phospholipid, phorbol esters 644999 2.7.11.15 additional information not activated by polycations 490911 2.7.11.15 additional information not effected by Ca2+ or Co2+ 645001 2.7.11.15 additional information partial agonists promote reduced receptor phosphorylation 490911 2.7.11.15 additional information phosphorylation activates the enzyme 672408 2.7.11.15 additional information phosphorylation by c-Src activates GRK2 661455 2.7.11.15 Oxytremorine requirement, agonist, muscarinic cholinergic receptor as substrate 645005 2.7.11.15 phosphatidic acid activates, phosphorylation of beta2-AR 645028 2.7.11.15 phosphatidylglycerol activates, phosphorylation of beta2-AR 645028 2.7.11.15 phosphatidylinositol activates, phosphorylation of beta2-AR, 6fold activation of phosphorylation of RRREEEEESAAA 645028 2.7.11.15 phosphatidylinositol 4,5-bisphosphate binding of GRK2 and GRK3 via their pleckstrin homology domains, activate the phosphorylation activity 661455 2.7.11.15 phosphatidylserine activates, phosphorylation of beta2-AR 645028 2.7.11.15 phosphatidylserine binding of GRK2 and GRK3 via their pleckstrin homology domains, activate the phosphorylation activity 661455 2.7.11.15 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 645028 2.7.11.15 PIP2 activates GRK2 through binding to its PH domain 677232 2.7.11.15 platelet activating factor requirement, agonist, beta-adrenergic receptor as substrate 490989 2.7.11.15 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 662401 2.7.11.15 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 645012