WordNet
- any of a large group of nitrogenous organic compounds that are essential constituents of living cells; consist of polymers of amino acids; essential in the diet of animals for growth and for repair of tissues; can be obtained from meat and eggs and milk and legumes; "a diet high in protein"
- a unit of force equal to the force exerted by gravity; used to indicate the force to which a body is subjected when it is accelerated (同)gee, g-force
- an enzyme that catalyzes the conversion of a proenzyme to an active enzyme
- the 7th letter of the Roman alphabet (同)g
- the basic unit of money in Papua New Guinea
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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2014/03/24 16:26:59」(JST)
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| protein kinase, cGMP-dependent, type I |
Crystallographic structure of the leucine zipper domain of human cGMP dependent protein kinase I beta.[1]
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| Identifiers |
| Symbol |
PRKG1 |
| Alt. symbols |
PRKGR1B, PRKG1B |
| Entrez |
5592 |
| HUGO |
9414 |
| OMIM |
176894 |
| RefSeq |
NM_006258 |
| UniProt |
Q13976 |
| Other data |
| Locus |
Chr. 10 q11.2 |
| protein kinase, cGMP-dependent, type II |
| Identifiers |
| Symbol |
PRKG2 |
| Entrez |
5593 |
| HUGO |
9416 |
| OMIM |
601591 |
| RefSeq |
NM_006259 |
| UniProt |
Q13237 |
| Other data |
| Locus |
Chr. 4 q13.1-21.1 |
cGMP-dependent protein kinase or Protein Kinase G (PKG) is a serine/threonine-specific protein kinase that is activated by cGMP. It phosphorylates a number of biologically important targets and is implicated in the regulation of smooth muscle relaxation, platelet function, sperm metabolism, cell division, and nucleic acid synthesis.
Contents
- 1 Genes and proteins
- 2 Tissue distribution
- 3 Role in cancer
- 4 See also
- 5 References
- 6 External links
Genes and proteins[edit]
PKG are serine/threonine kinases that are present in a variety of eukaryotes ranging from the unicellular organism Paramecium to humans. Two PKG genes, coding for PKG type I (PKG-I) and type II (PKG-II), have been identified in mammals. The N-terminus of PKG-I is encoded by two alternatively spliced exons that specify for the PKG-Iα and PKG-Iβ isoforms. PKG-Iβ is activated at ~10-fold higher cGMP concentrations than PKG-Iα. The PKG-I and PKG-II are homodimers of two identical subunits (~75 kDa and ~85 kDa, respectively) and share common structural features.
Each subunit is composed of three functional domains:
- (1) an N-terminal domain that mediates homodimerization, suppression of the kinase activity in the absence of cGMP, and interactions with other proteins including protein substrates
- (2) a regulatory domain that contains two non-identical cGMP-binding sites
- (3) a kinase domain that catalyzes the phosphate transfer from ATP to the hydroxyl group of a serine/threonine side chain of the target protein
Binding of cGMP to the regulatory domain induces a conformational change which stops the inhibition of the catalytic core by the N-terminus and allows the phosphorylation of substrate proteins. Whereas PKG-I is predominantly localized in the cytoplasm, PKG-II is anchored to the plasma membrane by N-terminal myristoylation.
Tissue distribution[edit]
In general, PKG-I and PKG-II are expressed in different cell types.
- PKG-I has been detected at high concentrations (above 0.1 µmol/L) in all types of smooth muscle cells (SMCs) including vascular SMCs and in platelets. Lower levels are present in vascular endothelium and cardiomyocytes. The enzyme is also expressed in fibroblasts, certain types of renal cells and leukocytes, and in specific regions of the nervous system, for example in the hippocampus, in cerebellar Purkinje cells, and in dorsal root ganglia. Neurons express either the PKG-Iα or the PKG-Iβ isoform, platelets predominantly Iβ, and both isoforms are present in smooth muscle.
- PKG-II has been detected in renal cells, zona glomerulosa cells of the adrenal cortex, Clara cells in distal airways, intestinal mucosa, pancreatic ducts, parotid and submandibular glands, chondrocytes, and several brain cell nuclei, but not in cardiac and vascular myocytes.
Specifically, in smooth muscle tissue, PKG promotes the opening of calcium-activated potassium channels, leading to cell hyperpolarization and relaxation, and blocks agonist activity of phospholipase C, reducing liberation of stored calcium ions by inositol triphosphate.
Role in cancer[edit]
Cancerous colon cells stop producing PKG, which apparently limits beta-catenin thus allowing the VEGF enzyme to solicit angiogenesis.[2]
See also[edit]
- cAMP-dependent protein kinase
References[edit]
- ^ PDB 3NMD; Casteel DE, Smith-Nguyen EV, Sankaran B, Roh SH, Pilz RB, Kim C (October 2010). "A crystal structure of the cyclic GMP-dependent protein kinase I{beta} dimerization/docking domain reveals molecular details of isoform-specific anchoring". J. Biol. Chem. 285 (43): 32684–8. doi:10.1074/jbc.C110.161430. PMID 20826808.
- ^ Kwon IK, Schoenlein PV, Delk J, Liu K, Thangaraju M, Dulin NO, Ganapathy V, Berger FG, Browning DD (April 2008). "Expression of cyclic guanosine monophosphate-dependent protein kinase in metastatic colon carcinoma cells blocks tumor angiogenesis". Cancer 112 (7): 1462–70. doi:10.1002/cncr.23334. PMID 18260092.
External links[edit]
- EC 2.7.11.12
- Cyclic GMP-Dependent Protein Kinases and the Cardiovascular System
- cGMP-Dependent Protein Kinases at the US National Library of Medicine Medical Subject Headings (MeSH)
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Kinases: Serine/threonine-specific protein kinases (EC 2.7.11-12)
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Serine/threonine-specific protein kinases (EC 2.7.11.1-EC 2.7.11.20)
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Serine/threonine-specific protein kinases (EC 2.7.11.21-EC 2.7.11.30)
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| Polo kinase (EC 2.7.11.21) |
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| Cyclin-dependent kinase (EC 2.7.11.22) |
- CDK1
- CDK2
- CDKL2
- CDK3
- CDK4
- CDK5
- CDKL5
- CDK6
- CDK7
- CDK8
- CDK9
- CDK10
- CDC2L5
- CRKRS
- PCTK1
- PCTK2
- PCTK3
- PFTK1
- CDC2L1
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| (RNA-polymerase)-subunit kinase (EC 2.7.11.23) |
- RPS6KA5
- RPS6KA4
- P70S6 kinase
- P70-S6 Kinase 1
- RPS6KB2
- RPS6KA2
- RPS6KA3
- RPS6KA1
- RPS6KC1
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| Mitogen-activated protein kinase (EC 2.7.11.24) |
- Extracellular signal-regulated
- MAPK1
- MAPK3
- MAPK4
- MAPK6
- MAPK7
- MAPK12
- MAPK15
- C-Jun N-terminal
- P38 mitogen-activated protein
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| MAP3K (EC 2.7.11.25) |
- MAP kinase kinase kinases
- MAP3K1
- MAP3K2
- MAP3K3
- MAP3K4
- MAP3K5
- MAP3K6
- MAP3K7
- MAP3K8
- RAFs
- MLKs
- MAP3K12
- MAP3K13
- MAP3K9
- MAP3K10
- MAP3K11
- MAP3K7
- ZAK
- CDC7
- MAP3K14
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| Tau-protein kinase (EC 2.7.11.26) |
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| (acetyl-CoA carboxylase) kinase (EC 2.7.11.27) |
-
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| Tropomyosin kinase (EC 2.7.11.28) |
-
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| Low-density-lipoprotein receptor kinase (EC 2.7.11.29) |
-
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| Receptor protein serine/threonine kinase (EC 2.7.11.30) |
- Bone morphogenetic protein receptors
- BMPR1
- BMPR1A
- BMPR1B
- BMPR2
- ACVR1
- ACVR1B
- ACVR1C
- ACVR2A
- ACVR2B
- ACVRL1
- Anti-Müllerian hormone receptor
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Dual-specificity kinases (EC 2.7.12)
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| MAP2K |
- MAP2K1
- MAP2K2
- MAP2K3
- MAP2K4
- MAP2K5
- MAP2K6
- MAP2K7
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- B
- enzm
- 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
- 2.1
- 3.1
- 4.1
- 5.1
- 6.1-3
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Intracellular signaling peptides and proteins
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| MAP |
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| Calcium |
- Intracellular calcium-sensing proteins
- Calcineurin
- Ca2+/calmodulin-dependent protein kinase
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| G protein |
| Heterotrimeric |
| cAMP: |
- Heterotrimeric G protein
- Adenylate cyclase
- cAMP
- 3',5'-cyclic-AMP phosphodiesterase
- Protein kinase A
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| cGMP: |
- Guanylate cyclase
- cGMP
- 3',5'-cyclic-GMP phosphodiesterase
- Protein kinase G
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- G beta-gamma complex Gβ
- Gγ
- GNGT1
- GNGT2
- GNG2
- GNG3
- GNG4
- GNG5
- GNG7
- GNG8
- GNG10
- GNG11
- GNG12
- GNG13
- BSCL2
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- G protein-coupled receptor kinase
- AMP-activated protein kinase
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| Monomeric |
- ARFs
- Rabs
- Ras
- Rhos
- Arfs
- Ran
- Rhebs
- Raps
- RGKs
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| Cyclin |
- Cyclin-dependent kinase inhibitor protein
- Cyclin-dependent kinase
- Cyclin
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| Lipid |
- Phosphoinositide phospholipase C
- Phospholipase C
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| Other protein kinase |
| Serine/threonine: |
- Casein kinase
- eIF-2 kinase
- Glycogen synthase kinase
- GSK1
- GSK2
- GSK-3
- GSK3A
- GSK3B
- IκB kinase
- Interleukin-1 receptor-associated kinase
- Lim kinase
- p21-activated kinases
- Rho-associated protein kinase
- Ribosomal s6 kinase
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| Tyrosine: |
- ZAP70
- Focal adhesion protein-tyrosine kinase
- BTK
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| both |
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| Other phosphoprotein phosphatase |
| Serine/threonine: |
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| Tyrosine: |
- protein tyrosine phosphatase: Receptor-like protein tyrosine phosphatase
- Sh2 domain-containing protein tyrosine phosphatase
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| both: |
- Dual-specificity phosphatase
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| Apoptosis |
- see apoptosis signaling pathway
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| GTP-binding protein regulators |
- see GTP-binding protein regulators
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| Other |
- Activating transcription factor 6
- Signal transducing adaptor protein
- I-kappa B protein
- Mucin-4
- Olfactory marker protein
- Phosphatidylethanolamine binding protein
- EDARADD
- PRKCSH
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see also deficiencies of intracellular signaling peptides and proteins
B trdu: iter (nrpl/grfl/cytl/horl), csrc (lgic, enzr, gprc, igsr, intg, nrpr/grfr/cytr), itra (adap, gbpr, mapk), calc, lipd; path (hedp, wntp, tgfp+mapp, notp, jakp, fsap, hipp, tlrp)
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UpToDate Contents
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English Journal
- Cyclic GMP-mediated memory enhancement in the object recognition test by inhibitors of phosphodiesterase-2 in mice.
- Lueptow LM1,2, Zhan CG3, O'Donnell JM4.
- Psychopharmacology.Psychopharmacology (Berl).2016 Feb;233(3):447-56. doi: 10.1007/s00213-015-4129-1. Epub 2015 Nov 2.
- RATIONALE AND OBJECTIVES: Cyclic nucleotide phosphodiesterase-2 (PDE2) is a potential therapeutic target for the treatment of cognitive dysfunction. Using the object recognition test (ORT), this study assessed the effects of two PDE2 inhibitors, Bay 60-7550 and ND7001, on learning and memory, and ex
- PMID 26525565
- The cyclic GMP/protein kinase G pathway as a therapeutic target in head and neck squamous cell carcinoma.
- Tuttle TR1, Mierzwa ML2, Wells SI3, Fox SR1, Ben-Jonathan N4.
- Cancer letters.Cancer Lett.2016 Jan 28;370(2):279-85. doi: 10.1016/j.canlet.2015.10.024. Epub 2015 Nov 10.
- Head and neck squamous cell carcinoma (HNSCC) is an aggressive disease with high mortality. Treatments, which can result in significant morbidity, have not substantially changed in three decades. The second messenger cyclic GMP (cGMP), which targets protein kinase G (PKG), is generated by guanylate
- PMID 26551887
Japanese Journal
- ROS Are Required for Mouse Spermatogonial Stem Cell Self-Renewal
- Morimoto Hiroko,Iwata Kazumi,Ogonuki Narumi,Inoue Kimiko,Ogura Atsuo,Kanatsu-Shinohara Mito,Morimoto Takeshi,Yabe-Nishimura Chihiro,Shinohara Takashi
- Cell Stem Cell 12(6), 774-786, 2013-06-00
- … SSCs depleted of ROS stopped proliferating, but they showed enhanced self-renewal when ROS levels were increased by the addition of hydrogen peroxide, which induced the phosphorylation of stress kinases p38 mitogen-activated protein kinase (MAPK) and c-jun N-terminal kinase (JNK). …
- NAID 120005285490
- Central role of the exchange factor GEF-H1 in TNF-α–induced sequential activation of Rac, ADAM17/TACE, and RhoA in tubular epithelial cells
- Waheed Faiza,Dan Qinghong,Amoozadeh Yasaman,Zhang Yuqian,Tanimura Susumu,Speight Pam,Kapus András,Szászi Katalin
- Molecular Biology of the Cell 24(7), 1068-1082, 2013-04-01
- … TACE activation requires the mitogen-activated protein kinase p38, which is activated through the small GTPase Rac. …
- NAID 120005231330
Related Links
- View and buy high purity products active at Protein Kinase G from Tocris Bioscience, the leading worldwide supplier of high performance life science reagents ... Protein Kinase G More Information »Protein Kinase G (PKG) is a cyclic ...
- Molecular Biochemistry I Signal Transduction Cascades Contents of this page: Kinases & phosphatases Protein Kinase A (cAMP-dependent protein kinase) G-protein signal cascade Structure of G-proteins Small GTP-binding ...
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★リンクテーブル★
[★]
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- protein kinase G、G-kinase
- 関
- サイクリックGMP依存性タンパク質リン酸化酵素、cGMP依存性タンパク質リン酸化酵素、サイクリックGMP依存性タンパク質キナーゼ、Gキナーゼ、サイクリックGMP依存性プロテインキナーゼ
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キナーゼ カイネース リン酸化酵素 phosphoenzyme phosphotransferase
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グラム
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