Biology:MAPK11
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Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
Mitogen-activated protein kinase 11 is an enzyme that in humans is encoded by the MAPK11 gene.[1][2]
Function
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 most closely related to p38 MAP kinase, both of which can be activated by proinflammatory cytokines and environmental stress. This kinase is activated through its phosphorylation by MAP kinase kinases (MKKs), preferably by MKK6. Transcription factor ATF2/CREB2 has been shown to be a substrate of this kinase.[2]
Interactions
MAPK11 has been shown to interact with HDAC3[3] and Promyelocytic leukemia protein.[4]
See also
References
- ↑ "Activation of the novel stress-activated protein kinase SAPK4 by cytokines and cellular stresses is mediated by SKK3 (MKK6); comparison of its substrate specificity with that of other SAP kinases". EMBO J. 16 (12): 3563–71. Aug 1997. doi:10.1093/emboj/16.12.3563. PMID 9218798.
- ↑ 2.0 2.1 "Entrez Gene: MAPK11 mitogen-activated protein kinase 11". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5600.
- ↑ "Histone deacetylase 3, a class I histone deacetylase, suppresses MAPK11-mediated activating transcription factor-2 activation and represses TNF gene expression". J. Immunol. 173 (6): 3979–90. Sep 2004. doi:10.4049/jimmunol.173.6.3979. PMID 15356147.
- ↑ "Promyelocytic leukemia is a direct inhibitor of SAPK2/p38 mitogen-activated protein kinase". J. Biol. Chem. 279 (39): 40994–1003. Sep 2004. doi:10.1074/jbc.M407369200. PMID 15273249.
External links
Further reading
- "Characterization of the structure and function of a new mitogen-activated protein kinase (p38beta)". J. Biol. Chem. 271 (30): 17920–6. 1996. doi:10.1074/jbc.271.30.17920. PMID 8663524.
- "Novel homologues of CSBP/p38 MAP kinase: activation, substrate specificity and sensitivity to inhibition by pyridinyl imidazoles". Biochem. Biophys. Res. Commun. 235 (3): 533–8. 1997. doi:10.1006/bbrc.1997.6849. PMID 9207191.
- "p38-2, a novel mitogen-activated protein kinase with distinct properties". J. Biol. Chem. 272 (31): 19509–17. 1997. doi:10.1074/jbc.272.31.19509. PMID 9235954.
- "Selective activation of p38 mitogen-activated protein (MAP) kinase isoforms by the MAP kinase kinases MKK3 and MKK6". J. Biol. Chem. 273 (3): 1741–8. 1998. doi:10.1074/jbc.273.3.1741. PMID 9430721.
- "PRAK, a novel protein kinase regulated by the p38 MAP kinase". EMBO J. 17 (12): 3372–84. 1998. doi:10.1093/emboj/17.12.3372. PMID 9628874.
- "Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB". EMBO J. 17 (15): 4426–41. 1998. doi:10.1093/emboj/17.15.4426. PMID 9687510.
- "The DNA sequence of human chromosome 22". Nature 402 (6761): 489–95. 1999. doi:10.1038/990031. PMID 10591208. Bibcode: 1999Natur.402..489D.
- "Constitutive activity and differential localization of p38alpha and p38beta MAPKs in adult mouse brain". J. Neurosci. Res. 60 (5): 623–31. 2000. doi:10.1002/(SICI)1097-4547(20000601)60:5<623::AID-JNR7>3.0.CO;2-4. PMID 10820433.
- "A Novel MAPK phosphatase MKP-7 acts preferentially on JNK/SAPK and p38 alpha and beta MAPKs". J. Biol. Chem. 276 (28): 26629–39. 2001. doi:10.1074/jbc.M101981200. PMID 11359773.
- "Nerve growth factor inhibits apoptosis in memory B lymphocytes via inactivation of p38 MAPK, prevention of Bcl-2 phosphorylation, and cytochrome c release". J. Biol. Chem. 276 (42): 39027–36. 2001. doi:10.1074/jbc.M102970200. PMID 11495898. https://flore.unifi.it/bitstream/2158/316195/1/316195.pdf.
- "The proto-oncoprotein Brx activates estrogen receptor beta by a p38 mitogen-activated protein kinase pathway". J. Biol. Chem. 276 (50): 46792–7. 2001. doi:10.1074/jbc.M106927200. PMID 11579095.
- "MAPKK-independent activation of p38alpha mediated by TAB1-dependent autophosphorylation of p38alpha". Science 295 (5558): 1291–4. 2002. doi:10.1126/science.1067289. PMID 11847341. Bibcode: 2002Sci...295.1291G.
- "Activation of p38 alpha MAPK enhances collagenase-1 (matrix metalloproteinase (MMP)-1) and stromelysin-1 (MMP-3) expression by mRNA stabilization". J. Biol. Chem. 277 (35): 32360–8. 2002. doi:10.1074/jbc.M204296200. PMID 12060661.
- "Stress-induced regulation of eukaryotic elongation factor 2 kinase by SB 203580-sensitive and -insensitive pathways". Biochem. J. 367 (Pt 2): 525–32. 2002. doi:10.1042/BJ20020916. PMID 12171600.
- "gp120-mediated induction of the MAPK cascade is dependent on the activation state of CD4(+) lymphocytes". Blood 100 (7): 2546–53. 2002. doi:10.1182/blood-2002-03-0819. PMID 12239168.
- "The transcriptional activator Mirk/Dyrk1B is sequestered by p38alpha/beta MAP kinase". J. Biol. Chem. 277 (51): 49438–45. 2002. doi:10.1074/jbc.M206840200. PMID 12384504.
- "Oxidative stress-induced apoptosis in dividing fibroblasts involves activation of p38 MAP kinase and over-expression of Bax: resistance of quiescent cells to oxidative stress". Apoptosis 8 (1): 91–100. 2003. doi:10.1023/A:1021657220843. PMID 12510156.
- "Neurotoxicity of pneumolysin, a major pneumococcal virulence factor, involves calcium influx and depends on activation of p38 mitogen-activated protein kinase". Neurobiol. Dis. 11 (3): 355–68. 2002. doi:10.1006/nbdi.2002.0561. PMID 12586546.
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