- MAPK8
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Mitogen-activated protein kinase 8 is an enzyme that in humans is encoded by the MAPK8 gene.[1][2]
The protein encoded by this gene is a member of the MAP kinase family. MAP kinases act as an integration point for multiple biochemical signals, and are involved in a wide variety of cellular processes such as proliferation, differentiation, transcription regulation and development. This kinase is activated by various cell stimuli, and targets specific transcription factors, and thus mediates immediate-early gene expression in response to cell stimuli. The activation of this kinase by tumor-necrosis factor alpha (TNF-alpha) is found to be required for TNF-alpha-induced apoptosis. This kinase is also involved in UV radiation-induced apoptosis, which is thought to be related to the cytochrome c-mediated cell death pathway. Studies of the mouse counterpart of this gene suggested that this kinase play a key role in T cell proliferation, apoptosis and differentiation. Four alternately spliced transcript variants encoding distinct isoforms have been reported.[3]
Contents
Interactions
MAPK8 has been shown to interact with SPIB,[4] DUSP1,[5] Activating transcription factor 2,[6][7][8][9] SH3BP5,[10] GSTP1,[11] MAPK8IP1,[12][13] MAP2K7,[9][14] CRK,[15] MAP2K4,[16][17][8][9][14] DUSP22,[18] Myc,[19] MAP3K2,[14] DUSP10,[20] REL,[21] MAPK8IP3,[22][23] IRS1,[24][25] MAP3K1[26] and C-jun.[27][28][1][29][30][21][31][9]
References
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- ^ a b c Cheng, J; Yang J, Xia Y, Karin M, Su B (Apr. 2000). "Synergistic Interaction of MEK Kinase 2, c-Jun N-Terminal Kinase (JNK) Kinase 2, and JNK1 Results in Efficient and Specific JNK1 Activation". Mol. Cell. Biol. (UNITED STATES) 20 (7): 2334–42. doi:10.1128/MCB.20.7.2334-2342.2000. ISSN 0270-7306. PMC 85399. PMID 10713157. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=85399.
- ^ Girardin, S E; Yaniv M (Jul. 2001). "A direct interaction between JNK1 and CrkII is critical for Rac1-induced JNK activation". EMBO J. (England) 20 (13): 3437–46. doi:10.1093/emboj/20.13.3437. ISSN 0261-4189. PMC 125507. PMID 11432831. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=125507.
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- ^ Park, Hee-Sae; Kim Mi-Sung, Huh Sung-Ho, Park Jihyun, Chung Jongkyeong, Kang Sang Sun, Choi Eui-Ju (Jan. 2002). "Akt (protein kinase B) negatively regulates SEK1 by means of protein phosphorylation". J. Biol. Chem. (United States) 277 (4): 2573–8. doi:10.1074/jbc.M110299200. ISSN 0021-9258. PMID 11707464.
- ^ Aoyama, K; Nagata M, Oshima K, Matsuda T, Aoki N (Jul. 2001). "Molecular cloning and characterization of a novel dual specificity phosphatase, LMW-DSP2, that lacks the cdc25 homology domain". J. Biol. Chem. (United States) 276 (29): 27575–83. doi:10.1074/jbc.M100408200. ISSN 0021-9258. PMID 11346645.
- ^ Noguchi, K; Kitanaka C, Yamana H, Kokubu A, Mochizuki T, Kuchino Y (Nov. 1999). "Regulation of c-Myc through phosphorylation at Ser-62 and Ser-71 by c-Jun N-terminal kinase". J. Biol. Chem. (UNITED STATES) 274 (46): 32580–7. doi:10.1074/jbc.274.46.32580. ISSN 0021-9258. PMID 10551811.
- ^ Tanoue, T; Moriguchi T, Nishida E (Jul. 1999). "Molecular cloning and characterization of a novel dual specificity phosphatase, MKP-5". J. Biol. Chem. (UNITED STATES) 274 (28): 19949–56. doi:10.1074/jbc.274.28.19949. ISSN 0021-9258. PMID 10391943.
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External Links
Further reading
- Davis RJ (2000). "Signal transduction by the JNK group of MAP kinases". Cell 103 (2): 239–52. doi:10.1016/S0092-8674(00)00116-1. PMID 11057897.
- Liu J, Lin A (2007). "Wiring the cell signaling circuitry by the NF-kappa B and JNK1 crosstalk and its applications in human diseases". Oncogene 26 (22): 3267–78. doi:10.1038/sj.onc.1210417. PMID 17496921.
PDB gallery 1jnk: THE C-JUN N-TERMINAL KINASE (JNK3S) COMPLEXED WITH MGAMP-PNP1pmn: Crystal structure of JNK3 in complex with an imidazole-pyrimidine inhibitor1pmq: The structure of JNK3 in complex with an imidazole-pyrimidine inhibitor1pmu: The crystal structure of JNK3 in complex with a phenantroline inhibitor1pmv: The structure of JNK3 in complex with a dihydroanthrapyrazole inhibitor1ukh: Structural basis for the selective inhibition of JNK1 by the scaffolding protein JIP1 and SP6001251uki: Structural basis for the selective inhibition of JNK1 by the scaffolding protein JIP1 and SP6001252b1p: inhibitor complex of JNK32exc: Inhibitor complex of JNK32g01: Pyrazoloquinolones as Novel, Selective JNK1 inhibitors2gmx: Selective Aminopyridine-Based C-Jun N-terminal Kinase inhibitors with cellular activity2h96: Discovery of Potent, Highly Selective, and Orally Bioavailable Pyridine Carboxamide C-jun NH2-terminal Kinase Inhibitors2no3: Novel 4-anilinopyrimidines as potent JNK1 Inhibitors2o0u: Crystal structure of human JNK3 complexed with N-{3-cyano-6-[3-(1-piperidinyl)propanoyl]-4,5,6,7-tetrahydrothieno[2,3-c]pyridin-2-yl}-1-naphthalenecarboxamide2o2u: Crystal structure of human JNK3 complexed with N-(3-cyano-4,5,6,7-tetrahydro-1-benzothien-2-yl)-2-fluorobenzamide2ok1: Crystal structure of JNK3 bound to N-benzyl-4-(4-(3-chlorophenyl)-1H-pyrazol-3-yl)-1H-pyrrole-2-carboxamideThis article incorporates text from the United States National Library of Medicine, which is in the public domain.
Kinases: Serine/threonine-specific protein kinases (EC 2.7.11-12) Serine/threonine-specific protein kinases (EC 2.7.11.1-EC 2.7.11.20) Non-specific serine/threonine protein kinases (EC 2.7.11.1)Pyruvate dehydrogenase kinase (EC 2.7.11.2)Dephospho-(reductase kinase) kinase (EC 2.7.11.3)(isocitrate dehydrogenase (NADP+)) kinase (EC 2.7.11.5)(tyrosine 3-monooxygenase) kinase (EC 2.7.11.6)Myosin-heavy-chain kinase (EC 2.7.11.7)Fas-activated serine/threonine kinase (EC 2.7.11.8)Goodpasture-antigen-binding protein kinase (EC 2.7.11.9)-IκB kinase (EC 2.7.11.10)cAMP-dependent protein kinase (EC 2.7.11.11)cGMP-dependent protein kinase (EC 2.7.11.12)Protein kinase C (EC 2.7.11.13)Rhodopsin kinase (EC 2.7.11.14)Beta adrenergic receptor kinase (EC 2.7.11.15)G-protein coupled receptor kinases (EC 2.7.11.16)Ca2+/calmodulin-dependent (EC 2.7.11.17)BRSK2, CAMK1, CAMK2A, CAMK2B, CAMK2D, CAMK2G, CAMK4, MLCK, CASK, CHEK1, CHEK2, DAPK1, DAPK2, DAPK3, STK11, MAPKAPK2, MAPKAPK3, MAPKAPK5, MARK1, MARK2, MARK3, MARK4, MELK, MKNK1, MKNK2, NUAK1, NUAK2, OBSCN, PASK, PHKG1, PHKG2, PIM1, PIM2, PKD1, PRKD2, PRKD3, PSKH1, SNF1LK2, KIAA0999, STK40, SNF1LK, SNRK, SPEG, TSSK2, Kalirin, TRIB1, TRIB2, TRIB3, TRIO, Titin, DCLK1Myosin light-chain kinase (EC 2.7.11.18)MYLK, MYLK2, MYLK3, MYLK4Phosphorylase kinase (EC 2.7.11.19)Elongation factor 2 kinase (EC 2.7.11.20)Serine/threonine-specific protein kinases (EC 2.7.11.21-EC 2.7.11.30) Polo kinase (EC 2.7.11.21)Cyclin-dependent kinase (EC 2.7.11.22)(RNA-polymerase)-subunit kinase (EC 2.7.11.23)Mitogen-activated protein kinase (EC 2.7.11.24)Extracellular signal-regulated (MAPK1, MAPK3, MAPK4, MAPK6, MAPK7, MAPK12, MAPK15), C-Jun N-terminal (MAPK8, MAPK9, MAPK10), P38 mitogen-activated protein (MAPK11, MAPK13, MAPK14)MAP3K (EC 2.7.11.25)Tau-protein kinase (EC 2.7.11.26)(acetyl-CoA carboxylase) kinase (EC 2.7.11.27)-Tropomyosin kinase (EC 2.7.11.28)-Low-density-lipoprotein receptor kinase (EC 2.7.11.29)-Receptor protein serine/threonine kinase (EC 2.7.11.30)Dual-specificity kinases (EC 2.7.12) This transferase article is a stub. You can help Wikipedia by expanding it.