Biology:MAPKAPK5
From HandWiki
 Generic protein structure example |
MAP kinase-activated protein kinase 5 is an enzyme that in humans is encoded by the MAPKAPK5 gene.[1][2] The protein encoded by this gene is a member of the serine/threonine kinase family. In response to cellular stress and proinflammatory cytokines, this kinase is activated through its phosphorylation by MAP kinases, including MAPK1/ERK, MAPK14/p38-alpha, and MAPK11/p38-beta. In vitro, this kinase phosphorylates heat shock protein HSP27 at its physiologically relevant sites. Two alternately-spliced transcript variants of this gene encoding distinct isoforms have been reported.[2]
A link between Alzheimer's disease and reduced levels of MAPKAPK5 has been proposed. Clinical trials may confirm if this is the case.
References
- ↑ "PRAK, a novel protein kinase regulated by the p38 MAP kinase". EMBO J 17 (12): 3372–84. Jul 1998. doi:10.1093/emboj/17.12.3372. PMID 9628874.
- ↑ 2.0 2.1 "Entrez Gene: MAPKAPK5 mitogen-activated protein kinase-activated protein kinase 5". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8550.
Further reading
- "Identification of phosphorylation sites of human 85-kDa cytosolic phospholipase A2 expressed in insect cells and present in human monocytes.". J. Biol. Chem. 271 (12): 6987–97. 1996. doi:10.1074/jbc.271.12.6987. PMID 8636128.
- "Identification of the phosphorylation sites of cytosolic phospholipase A2 in agonist-stimulated human platelets and HeLa cells.". J. Biol. Chem. 273 (8): 4449–58. 1998. doi:10.1074/jbc.273.8.4449. PMID 9468497.
- "MAPKAPK5, a novel mitogen-activated protein kinase (MAPK)-activated protein kinase, is a substrate of the extracellular-regulated kinase (ERK) and p38 kinase.". Biochem. Biophys. Res. Commun. 243 (2): 492–6. 1998. doi:10.1006/bbrc.1998.8135. PMID 9480836.
- "p62 functions as a p38 MAP kinase regulator.". Biochem. Biophys. Res. Commun. 269 (2): 521–5. 2000. doi:10.1006/bbrc.2000.2333. PMID 10708586.
- "Serine 727 phosphorylation and activation of cytosolic phospholipase A2 by MNK1-related protein kinases.". J. Biol. Chem. 275 (48): 37542–51. 2001. doi:10.1074/jbc.M003395200. PMID 10978317.
- "Recurrent variable region gene usage and somatic mutation in the human antibody response to the capsular polysaccharide of Streptococcus pneumoniae type 23F.". Infect. Immun. 70 (8): 4083–91. 2002. doi:10.1128/IAI.70.8.4083-4091.2002. PMID 12117915.
- "Analysis of V(lambda)-J(lambda) expression in plasma cells from primary (AL) amyloidosis and normal bone marrow identifies 3r (lambdaIII) as a new amyloid-associated germline gene segment.". Blood 100 (3): 948–53. 2002. doi:10.1182/blood-2002-01-0114. PMID 12130507.
- "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.
- "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. 2003. doi:10.1073/pnas.242603899. PMID 12477932. Bibcode: 2002PNAS...9916899M.
- "Regulation of PRAK subcellular location by p38 MAP kinases.". Mol. Biol. Cell 14 (6): 2603–16. 2004. doi:10.1091/mbc.E02-08-0538. PMID 12808055.
- "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. 2004. doi:10.1038/ng1285. PMID 14702039.
- "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. 2004. doi:10.1101/gr.2596504. PMID 15489334.
- "PRAK is essential for ras-induced senescence and tumor suppression.". Cell 128 (2): 295–308. 2007. doi:10.1016/j.cell.2006.11.050. PMID 17254968.
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