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Information on EC 2.7.11.12 - cGMP-dependent protein kinase and Organism(s) Rattus norvegicus and UniProt Accession Q64595
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2.7.11.12 cGMP-dependent protein kinaseIUBMB Comments
CGMP is required to activate this enzyme. The enzyme occurs as a dimer in higher eukaryotes. The C-terminal region of each polypeptide chain contains the catalytic domain that includes the ATP and protein substrate binding sites. This domain catalyses the phosphorylation by ATP to specific serine or threonine residues in protein substrates . The enzyme also has two allosteric cGMP-binding sites (sites A and B). Binding of cGMP causes a conformational change that is associated with activation of the kinase .
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Word Map
- 2.7.11.12
- cyclase
-
guanylyl
-
guanylate
-
camp-dependent
- phosphodiesterase
- endothelial
- artery
-
natriuretic
- pka
- cardiac
- nitroprusside
- 8-br-cgmp
-
contractile
- atrial
- phosphoprotein
-
myocytes
-
vasodilation
- 8-bromo-cgmp
-
l-name
-
no-induced
- sildenafil
-
vasorelaxation
-
l-type
-
cgmp-mediated
-
vasodilator-stimulated
-
patch-clamp
-
membrane-permeable
- snap
- vasp
-
cell-attached
- monophosphorothioate
- nonoate
-
cgmp-independent
- zaprinast
-
no-cgmp
-
iberiotoxin
-
atp-sensitive
-
1h-1,2,4oxadiazolo4,3-aquinoxalin-1-one
-
large-conductance
- s-nitroso-n-acetylpenicillamine
-
8-bromo-cyclic
-
cgmp-specific
- cak
- drug development
- 8-bromoguanosine
- rp-camps
-
cgmp-inhibited
-
nitrovasodilators
- medicine
- mypt1
- pharmacology
-
no-sensitive
-
oxide-cyclic
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
Reaction Schemes
+
a [protein]-(L-serine/L-threonine)
=
+
a [protein]-(L-serine/L-threonine) phosphate
Synonyms
cgmp-dependent protein kinase, protein kinase g, cyclic gmp-dependent protein kinase, cgkii, pkg-i, cgmp kinase, prkg1, pkg ii, cgk ii, cgmp-dependent protein kinase i, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CGK
CGK 1 alpha
-
-
-
-
CGK 1 beta
-
-
-
-
CGKI-alpha
-
-
-
-
cGKI-beta
-
-
-
-
cGKII
cGMP-dependent protein kinase
Foraging protein
-
-
-
-
PKG
-
-
PKGIgamma
-
proteolytically cleaved cGMP-dependent protein kinase I fragment
protein kinase G
-
-
-
-
Type II cGMP-dependent protein kinase
-
-
-
-
CGK
-
-
-
-
cGKII
-
-
-
-
cGMP-dependent protein kinase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
ATP:protein phosphotransferase (cGMP-dependent)
CGMP is required to activate this enzyme. The enzyme occurs as a dimer in higher eukaryotes. The C-terminal region of each polypeptide chain contains the catalytic domain that includes the ATP and protein substrate binding sites. This domain catalyses the phosphorylation by ATP to specific serine or threonine residues in protein substrates [3]. The enzyme also has two allosteric cGMP-binding sites (sites A and B). Binding of cGMP causes a conformational change that is associated with activation of the kinase [4].
CAS REGISTRY NUMBER
COMMENTARY
141588-27-4
-
141588-27-4
cGMP-dependent protein kinase
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + BKCa channel protein
ADP + BKCa channel phosphoprotein
-
phosphorylation at Ser691, Ser873, and Ser1112 on recombinant Mus musculus BKCa channels expressed in Rattus norvegicus aortic A7r5 smooth muscle cells or in humn in HEK 293 cells
-
-
?
ATP + GluA1 protein
ADP + GluA1 phosphoprotein
-
phosphorylation at Ser845 by type II cGMP-dependent protein kinase
-
-
?
ATP + glycogen synthase kinase-3
ADP + phosphorylated glycogen synthase kinase 3
-
phosphorylation at Ser9 by PKGI and PKGII inhibiting the glycogen synthase kinase-3 inducing dephosphorylation of C/EBPbeta, i.e. the CCAAT enhancer-binding protein beta, important in regulation of gene expression during cell proliferation, differentiation, and apoptosis
-
-
?
ATP + glycogen synthase kinase3
ADP + phosphorylated glycogen synthase kinase 3
-
phosphorylation at Ser9 by PKGI and PKGII inhibiting the glycogen synthase kinase-3, substrate phosphorylation site mapping
-
-
?
ATP + steroidogenic acute regulatory protein
ADP + phosphorylated steroidogenic acute regulatory protein
-
i.e. StAR, recombinant GST-tagged substrate expressed in HEK-293 cells, phosphorylation in vitro at Ser55, Ser56, and Ser99
-
-
?
ATP + target membrane SNARe complex
ADP + phosphorylated target membrane SNARe complex
-
the enzyme is involved in regulation of degranulation of leukocytes by phosphorylation of target membrane SNARe complex together with the phosphoinositide 3-kinase
-
-
?
ATP + transient receptor potential channel 6
ADP + phosphorylated transient receptor potential channel 6
-
PKG phosphorylation is reduced in transient receptor potential channel 6 mutant T69A
-
-
?
ATP + CFTR
ADP + phosphorylated CFTR
-
phosphorylation leads to stimulation of chloride channels
-
-
?
ATP + CFTR
ADP + phosphorylated CFTR
-
phosphorylation by cGKI and cGKII
-
-
?
ATP + Na+/K+ ATPase
ADP + phosphorylated Na+/K+ ATPase
-
the enzyme has a positive regulatory function on the ion pump activity induced by No and glutamate via increased cGMP, overview
-
-
?
additional information
?
-
-
alternative splicing of PKGI in angiotensin-hypertension, mechanism for nitrate tolerance in vascular smooth muscle
-
-
?
additional information
?
-
-
cyclic GMP-dependent protein kinase regulates CCAAT enhancer-binding protein beta functions through inhibition of glycogen synthase kinase-3
-
-
?
additional information
?
-
-
PKGII regulates basal level of aldosterone production by zona glomerulosa cells without increasing expression of the steroidogenic acute regulatory protein gene
-
-
?
additional information
?
-
-
the enzyme is required for adenosine-induced dilation of intracerebral arterioles and thus in regulation of cerebral blood flow, mechanism
-
-
?
additional information
?
-
-
the enzyme performs autophosphorylation at serines 110, 114, 117, 126, and 445 and at Thr109 in vitro and in vivo
-
-
?
additional information
?
-
-
the phorbol myristate acetate-stimulated PKC isozyme activates BKCa channels in rat pulmonary arterial smooth muscle via cGMP-dependent protein kinase
-
-
?
additional information
?
-
-
cGMP-activated PKGI inhibits TAB1-p38 mitogen-activated protein kinase apoptosis signaling in cardiac myocytes and protects them from ischemia and reperfusion injury, cGMP-activated PKG I does not inhibit MKK3- and MKK6-p38 MAPK signaling, overview
-
-
?
additional information
?
-
-
PKG I plays a major role in vascular homeostasis by mediating smooth muscle relaxation in response to nitric oxide, regulation of PKG I expression by Rho and Kruppel-like transcription factor-4, RhoA is involved in decreased PKG I levels in vascular smooth muscle cells found in some models of hypertension and vascular injury, overview
-
-
?
additional information
?
-
-
transcriptional regulation by the cgMP/PKG pathway affects the amount of IL-6 expression, cGMP-induced PKG activates the IL-6 promoter involving cis-acting DNA elements and transcription factors, the activation is prevented by actinomycin D, regulation system, overview
-
-
?
additional information
?
-
-
PKG phosphorylates several substrates and interacts, by engaging its N-terminal, with numerous proteins
-
-
?
additional information
?
-
-
serine to alanine substitutions at 3 of 6 putative cGKI phosphorylation sites, Ser691, Ser873, and Ser1112, in the BKCa alpha-subunit and mutant expression in A7r5 cells individually reduce direct channel phosphorylation by 25-60% and block BKCa activation by either an NO donor or a membrane-permeable cGMP by 80-100%
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + CFTR
ADP + phosphorylated CFTR
-
phosphorylation leads to stimulation of chloride channels
-
-
?
ATP + GluA1 protein
ADP + GluA1 phosphoprotein
-
phosphorylation at Ser845 by type II cGMP-dependent protein kinase
-
-
?
ATP + glycogen synthase kinase-3
ADP + phosphorylated glycogen synthase kinase 3
-
phosphorylation at Ser9 by PKGI and PKGII inhibiting the glycogen synthase kinase-3 inducing dephosphorylation of C/EBPbeta, i.e. the CCAAT enhancer-binding protein beta, important in regulation of gene expression during cell proliferation, differentiation, and apoptosis
-
-
?
ATP + Na+/K+ ATPase
ADP + phosphorylated Na+/K+ ATPase
-
the enzyme has a positive regulatory function on the ion pump activity induced by No and glutamate via increased cGMP, overview
-
-
?
ATP + target membrane SNARe complex
ADP + phosphorylated target membrane SNARe complex
-
the enzyme is involved in regulation of degranulation of leukocytes by phosphorylation of target membrane SNARe complex together with the phosphoinositide 3-kinase
-
-
?
additional information
?
-
-
alternative splicing of PKGI in angiotensin-hypertension, mechanism for nitrate tolerance in vascular smooth muscle
-
-
?
additional information
?
-
-
cyclic GMP-dependent protein kinase regulates CCAAT enhancer-binding protein beta functions through inhibition of glycogen synthase kinase-3
-
-
?
additional information
?
-
-
PKGII regulates basal level of aldosterone production by zona glomerulosa cells without increasing expression of the steroidogenic acute regulatory protein gene
-
-
?
additional information
?
-
-
the enzyme is required for adenosine-induced dilation of intracerebral arterioles and thus in regulation of cerebral blood flow, mechanism
-
-
?
additional information
?
-
-
the enzyme performs autophosphorylation at serines 110, 114, 117, 126, and 445 and at Thr109 in vitro and in vivo
-
-
?
additional information
?
-
-
the phorbol myristate acetate-stimulated PKC isozyme activates BKCa channels in rat pulmonary arterial smooth muscle via cGMP-dependent protein kinase
-
-
?
additional information
?
-
-
cGMP-activated PKGI inhibits TAB1-p38 mitogen-activated protein kinase apoptosis signaling in cardiac myocytes and protects them from ischemia and reperfusion injury, cGMP-activated PKG I does not inhibit MKK3- and MKK6-p38 MAPK signaling, overview
-
-
?
additional information
?
-
-
PKG I plays a major role in vascular homeostasis by mediating smooth muscle relaxation in response to nitric oxide, regulation of PKG I expression by Rho and Kruppel-like transcription factor-4, RhoA is involved in decreased PKG I levels in vascular smooth muscle cells found in some models of hypertension and vascular injury, overview
-
-
?
additional information
?
-
-
transcriptional regulation by the cgMP/PKG pathway affects the amount of IL-6 expression, cGMP-induced PKG activates the IL-6 promoter involving cis-acting DNA elements and transcription factors, the activation is prevented by actinomycin D, regulation system, overview
-
-
?
additional information
?
-
-
PKG phosphorylates several substrates and interacts, by engaging its N-terminal, with numerous proteins
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(9S,10R,12R)-2,3,9,10,11,12-hexahydro-10-methoxy-2,9-dimethyl-1-oxo-9,12-epoxy-1H-diindolo [1,2,3-fg:',2',1'-kl]pyrrolo [3,4-i][1,6]benzodiazocine-10-carboxylic acid methyl ester
-
KT-5823, specific PKG inhibitor
angiotensin
-
causes a decrease in expression of isozyme cGKIalpha, and an increase in expression of isozyme cGKIbeta
Rp-8-Br-cGMP
-
in vivo inhibition in leukemia cells causes reduced agonist-stimulated beta-hexosaminidase release and abolishes vesicular fusion with the plasma membrane
Rp-8-p-CPT-cGMP
-
i.e. Rp-8-(4-chlorophenylthio)guanosine 3',5'-cyclic monophosphate
KT5823
-
in vivo inhibition in leukemia cells causes reduced agonist-stimulated beta-hexosaminidase release and abolishes vesicular fusion with the plasma membrane
KT5823
-
effect of KT5823 is abolished in the presence of the nonselective cyclic nucleotide PDE inhibitor 3-isobutyl-1-methylxantine or the selective cGMP-PDE5 inhibitor sildenafil
additional information
-
PKGII inhibition inhibits aldosterone production
-
additional information
-
Rho and Krueppel-like transcription factor-4 KLF4, a bound nuclear protein, suppress PKG I expression requiring Sp1 consensus sequences in the PKG I promoter, suppression in a in a cell density-dependent manner
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
8-pCPT-CGMP
-
i.e. 8-(4-chlorophenylthio)guanosine 3',5'-cyclic monophosphate
adenosine
-
adenosine-induced vasodilation in cerebral microvessesls involves cGMP and cGMP-dependent protein kinase
angiotensin
-
causes an increase in expression of isozyme cGKIbeta, and a decrease in expression of isozyme cGKIalpha
calcium/calmodulin-dependent kinase II
-
mediates NO-elicited PKG activation
-
N2,2'-O-dibutyryl-cGMP
-
a membrane-permeable cGMP analogue, activates cGKI
Sp-8-pCPT-cGMPS
-
cyclic guanosine monophosphate-dependent protein kinase activator, selective for PKG
8-bromo-cGMP
-
activation of cGKII by 8-bromo-cGMP enhances the surface expression of GluA1, whereas its inhibition or suppression effectively diminishes the expression of this protein at the cell surface
cGMP
-
-
cGMP
-
activates native and recombinant enzyme, the activation of recombinant cGKII is reduced because the enzyme already partially phosphorylated
cGMP
-
cGMP-dependent activation of GKII depends on NO produced by nitric oxide synthase upon NMDA receptor activation
additional information
-
glutamate induced NO, and increased NO release from sodium nitroprusside and S-nitroso-N-acetylpenicillamine increase cGMP level which increases PKG activity, overview
-
additional information
-
NO activates the enzyme through elevation of cGMP concentration, reduced in hypertensive rats due to a shift in relation of cGKIalpha to cGKIbeta
-
additional information
-
the activity of transient receptor potential channel 6 channels is markedly suppressed by PKG activation
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
activity in vasodilation of arterioles measured in passive diameter
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.8 - 7.6
-
assay at, study of pH responsiveness of asteriole enzymes in vivo
7.4
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
adrenal, PKGI, expression of PKGII is restricted to adrenal zona glomerulosa cells
additional information
-
PKG-I expression is reduced or even lost in many primary cultured and passaged cells, e.g. vascular smooth muscle cells and endothelial cells
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
additional information
-
the PKG-Ialpha isoform is more sensitive to ubiquitination compared with the PKG-Ibeta isoform
malfunction
-
acute inhibition of cGKI prevents stimulus-evoked enhancement of BKCa channel activity
malfunction
-
PKG inhibition also potentiates the effect of SNAP on global cGMP levels and fully blocks the increase in cGMP-PDE5 activity
metabolism
-
cGMP-dependent protein kinase exerts a feedback control on cGMP concentration contributing to its intracellular compartmentation
metabolism
-
molecular mechanisms governing the transcriptional and posttranscriptional regulation of PKG-I expression in vascular smooth muscle cells, overview
physiological function
-
cGMP-dependent protein kinase type I is an essential regulator of cellular function in blood vessels throughout the body
physiological function
-
cGMP production activates cGKII and induces the phosphorylation of GluA1, promoting its accumulation in the plasma membrane. Phosphorylation of GluA1 at Ser845 by type II cGMP-dependent protein kinase augments the surface expression of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptors at both synaptic and extrasynaptic sites. Activation of cGKII by 8-Br-cGMP enhances the surface expression of GluA1, whereas its inhibition or suppression effectively diminishes the expression of this protein at the cell surface, overview
physiological function
-
cGMP-dependent protein kinase exerts a feedback control on cGMP concentration contributing to its intracellular compartmentation, negative feedback of PKG on sGC-cGMP signaling attributable to PDE5 activation, kinetics and overview. PKG inhibition decreases and PKG activation increases cGMP-gated current. PKG activation in adult cardiomyocytes limits the accumulation of cGMP induced by NO donors via PDE5 stimulation but increases that induced by natriuretic peptides
physiological function
-
PKG-I is a serine/threonine-specific protein kinase that is activated by the NO/sGC/cGMP system. PKG-I is involved in many cell functions, such as relaxation, platelet aggregation, remodelling, hypertrophy, apoptosis, differentiation, neuronal plasticity, and erectile dysfunction
physiological function
-
the activity of large conductance, Ca2+-activated K+ channels, i.e. BKCa channels, can be increased after modulation by type I cGMP-dependent protein kinase via nitric oxide/cGMP signaling
physiological function
-
the nuclear enzyme regulates the vascular smooth muscle cell phenotype
physiological function
-
isoform PKG2 is a key regulator of osteoblast proliferation and post-natal bone formation
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). KGP2_RAT
762
0
87182
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
additional information
-
the PKG-Ialpha isoform is more sensitive to ubiquitination compared with the PKG-Ibeta isoform
phosphoprotein
-
the enzyme performs autophosphorylation at serines 110, 114, 117, 126, and 445 and at Thr109, phosphorylation at Ser110 and Ser97 of the recombinant enzyme expressed in Sf9 insect cells, phosphorylation site mapping
phosphoprotein
-
PKG-I isoforms undergo autophosphorylation, in response to sustained activation/autophosphorylation, PKG-I might becomes ubiquitinated and degraded
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K482A
-
site-directed mutagenesis, transfection of the catalytically inactive PKGII mutant inhibits aldosterone production in zona glomerulosa cells
R242Q
-
the partially activated mutant enzyme expressed in primary osteoblasts of transgenic mice shows a 2-3fold increase in basal and total isoform PKG2 activity; they proliferate faster and are resistant to apoptosis compared to cells from wild type mice
S110A/S114A/S445A
-
site-directed mutagenesis, the mutant shows 60% reduced autophosphorylation activity compared to the wild-type GKII
additional information
additional information
-
constructing PKG I-DELTAN1-92, a PKG I mutant lacking the N-terminal 92 amino acids
additional information
-
siRNA-mediated down-regulation of RhoA derepresses PKG I expression
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
co-expression of FLAG-tagged p38alpha MAPK, and PKG Ialpha or PKG I-DELTAN1-92 plasmid expression vectors, and stimulation with 8-pCPT-cGMP, in HEK-293 cells
-
expression of PKGI and PKGII in UMR106 cells, PKGI expression enhances the glycosynthase kinase-3 phosphorylation to a greater extent than PKGII
-
transient co-expression of cGKI and substrate BKCa channels in HEK 293 cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
cGMP-dependent protein kinase activity is restored in vascular smooth muscle cells by transfection of primary rat aortic smooth muscle cells with an expression vector coding for the catalytic domain of bovine PKG
-
cGMP-dependent protein kinase is downregulated in vessels from diabetic animals or in vascular smooth muscle cells exposed to high-glucose conditions
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
all-D-YGRKKRRQRRRPPLRKKKKKH may help our understanding of how blood vessels constrict and dilate and may also aid the development of new strategies and therapeutic agents targeted to the prevention and treatment of vascular disorders
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jarchau, T.; Hausler, C.; Markert, T.; Pohler, D.; Vanderkerckhove, J.; De Jonge, H.R.; Lohmann, S.M.; Walter, U.
Cloning, expression, and in situ localization of rat intestinal cGMP-dependent protein kinase II
Proc. Natl. Acad. Sci. USA
91
9426-9430
1994
Rattus norvegicus (Q64595)
Barman, S.A.; Zhu, S.; White, R.E.
PKC activates BKCa channels in rat pulmonary arterial smooth muscle via cGMP-dependent protein kinase
Am. J. Physiol.
286
L1275-1281
2004
Rattus norvegicus
Munhoz, C.D.; Kawamoto, E.M.; de Sa Lima, L.; Lepsch, L.B.; Glezer, I.; Marcourakis, T.; Scavone, C.
Glutamate modulates sodium-potassium-ATPase through cyclic GMP and cyclic GMP-dependent protein kinase in rat striatum
Cell Biochem. Funct.
23
115-123
2005
Rattus norvegicus
Gerzanich, V.; Ivanov, A.; Ivanova, S.; Yang, J.B.; Zhou, H.; Dong, Y.; Simard, J.M.
Alternative splicing of cGMP-dependent protein kinase I in angiotensin-hypertension: novel mechanism for nitrate tolerance in vascular smooth muscle
Circ. Res.
93
805-812
2003
Rattus norvegicus
Schlossmann, J.; Hofmann, F.
cGMP-dependent protein kinases in drug discovery
Drug Discov. Today
10
627-634
2005
Homo sapiens, Mus musculus, Rattus norvegicus
Vaandrager, A.B.; Hogema, B.M.; Edixhoven, M.; van den Burg, C.M.; Bot, A.G.; Klatt, P.; Ruth, P.; Hofmann, F.; Van Damme, J.; Vandekerckhove, J.; de Jonge, H.R.
Autophosphorylation of cGMP-dependent protein kinase type II
J. Biol. Chem.
278
28651-28658
2003
Homo sapiens, Mus musculus, Rattus norvegicus
Gambaryan, S.; Butt, E.; Marcus, K.; Glazova, M.; Palmetshofer, A.; Guillon, G.; Smolenski, A.
cGMP-dependent protein kinase type II regulates basal level of aldosterone production by zona glomerulosa cells without increasing expression of the steroidogenic acute regulatory protein gene
J. Biol. Chem.
278
29640-29648
2003
Rattus norvegicus
Zhao, X.; Zhuang, S.; Chen, Y.; Boss, G.R.; Pilz, R.B.
Cyclic GMP-dependent protein kinase regulates CCAAT enhancer-binding protein beta functions through inhibition of glycogen synthase kinase-3
J. Biol. Chem.
280
32683-32692
2005
Rattus norvegicus
West, G.A.; Meno, J.R.; Nguyen, T.S.; Ngai, A.C.; Simard, J.M.; Winn, H.R.
cGMP-dependent and not cAMP-dependent kinase is required for adenosine-induced dilation of intracerebral arterioles
J. Cardiovasc. Pharmacol.
41
444-451
2003
Rattus norvegicus
Zeng, Y.; Zhuang, S.; Gloddek, J.; Tseng, C.C.; Boss, G.R.; Pilz, R.B.
Regulation of cGMP-dependent protein kinase expression by Rho and Kruppel-like transcription factor-4
J. Biol. Chem.
281
16951-16961
2006
Rattus norvegicus
Fiedler, B.; Feil, R.; Hofmann, F.; Willenbockel, C.; Drexler, H.; Smolenski, A.; Lohmann, S.M.; Wollert, K.C.
cGMP-dependent protein kinase type I inhibits TAB1-p38 mitogen-activated protein kinase apoptosis signaling in cardiac myocytes
J. Biol. Chem.
281
32831-32840
2006
Mus musculus, Mus musculus C57BL/6, Rattus norvegicus
Nanamori, M.; Chen, J.; Du, X.; Ye, R.D.
Regulation of leukocyte degranulation by cGMP-dependent protein kinase and phosphoinositide 3-kinase: potential roles in phosphorylation of target membrane SNARE complex proteins in rat mast cells
J. Immunol.
178
416-427
2007
Rattus norvegicus
Broderick, K.E.; Zhang, T.; Rangaswami, H.; Zeng, Y.; Zhao, X.; Boss, G.R.; Pilz, R.B.
Guanosine 3,5-cyclic monophosphate (cGMP)/cGMP-dependent protein kinase induce interleukin-6 transcription in osteoblasts
Mol. Endocrinol.
21
1148-1162
2007
Homo sapiens, Rattus norvegicus
Chen, G.D.; Peng, M.L.; Wang, P.Y.; Lee, S.D.; Chang, H.M.; Pan, S.F.; Chen, M.J.; Tung, K.C.; Lai, C.Y.; Lin, T.B.
Calcium/calmodulin-dependent kinase II mediates NO-elicited PKG activation to participate in spinal reflex potentiation in anesthetized rats
Am. J. Physiol. Regul. Integr. Comp. Physiol.
294
R487-R493
2008
Rattus norvegicus
Hernandez-Pacheco, A.; Araiza-Saldana, C.I.; Granados-Soto, V.; Mixcoatl-Zecuatl, T.
Possible participation of the nitric oxide-cyclic GMP-protein kinase G-K+ channels pathway in the peripheral antinociception of melatonin
Eur. J. Pharmacol.
596
70-76
2008
Rattus norvegicus
Boran, M.S.; Baltrons, M.A.; Garcia, A.
The ANP-cGMP-protein kinase G pathway induces a phagocytic phenotype but decreases inflammatory gene expression in microglial cells
Glia
56
394-411
2008
Rattus norvegicus
Takahashi, S.; Lin, H.; Geshi, N.; Mori, Y.; Kawarabayashi, Y.; Takami, N.; Mori, M.X.; Honda, A.; Inoue, R.
Nitric oxide-cGMP-protein kinase G pathway negatively regulates vascular transient receptor potential channel TRPC6
J. Physiol.
586
4209-4223
2008
Homo sapiens, Rattus norvegicus
Wang, S.; Li, Y.
Expression of constitutively active cGMP-dependent protein kinase inhibits glucose-induced vascular smooth muscle cell proliferation
Am. J. Physiol. Heart Circ. Physiol.
297
H2075-H2083
2009
Bos taurus, Homo sapiens, Mus musculus, Rattus norvegicus
Nickl, C.K.; Raidas, S.K.; Zhao, H.; Sausbier, M.; Ruth, P.; Tegge, W.; Brayden, J.E.; Dostmann, W.R.
(D)-Amino acid analogues of DT-2 as highly selective and superior inhibitors of cGMP-dependent protein kinase Ialpha
Biochim. Biophys. Acta
1804
524-532
2010
Homo sapiens, Mus musculus, Rattus norvegicus
Incontro, S.; Ciruela, F.; Ziff, E.; Hofmann, F.; Sanchez-Prieto, J.; Torres, M.
The type II cGMP dependent protein kinase regulates GluA1 levels at the plasma membrane of developing cerebellar granule cells
Biochim. Biophys. Acta
1833
1820-1831
2013
Rattus norvegicus, Rattus norvegicus Wistar
Sellak, H.; Choi, C.S.; Dey, N.B.; Lincoln, T.M.
Transcriptional and post-transcriptional regulation of cGMP-dependent protein kinase (PKG-I): pathophysiological significance
Cardiovasc. Res.
97
200-207
2013
Bos taurus, Oryctolagus cuniculus, Ovis aries, Homo sapiens, Mus musculus, Rattus norvegicus, Sus scrofa
Castro, L.R.; Schittl, J.; Fischmeister, R.
Feedback control through cGMP-dependent protein kinase contributes to differential regulation and compartmentation of cGMP in rat cardiac myocytes
Circ. Res.
107
1232-1240
2010
Rattus norvegicus
Kyle, B.D.; Hurst, S.; Swayze, R.D.; Sheng, J.; Braun, A.P.
Specific phosphorylation sites underlie the stimulation of a large conductance, Ca2+-activated K+ channel by cGMP-dependent protein kinase
FASEB J.
27
2027-2038
2013
Bos taurus, Rattus norvegicus
Chen, J.; Roberts, J.D.
cGMP-dependent protein kinase I gamma encodes a nuclear localization signal that regulates nuclear compartmentation and function
Cell. Signal.
26
2633-2644
2014
Rattus norvegicus
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