MAPKAPK2
Mitogen-activated protein kinase-activated protein kinase 2 | |||||||||||||
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File:PBB Protein MAPKAPK2 image.jpg PDB rendering based on 1kwp. | |||||||||||||
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Identifiers | |||||||||||||
Symbols | MAPKAPK2 ; | ||||||||||||
External IDs | Template:OMIM5 Template:MGI HomoloGene: 56412 | ||||||||||||
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RNA expression pattern | |||||||||||||
File:PBB GE MAPKAPK2 201460 at tn.png | |||||||||||||
File:PBB GE MAPKAPK2 201461 s at tn.png | |||||||||||||
File:PBB GE MAPKAPK2 215050 x at tn.png | |||||||||||||
More reference expression data | |||||||||||||
Orthologs | |||||||||||||
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Species | Human | Mouse | |||||||||||
Entrez | n/a | n/a | |||||||||||
Ensembl | n/a | n/a | |||||||||||
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RefSeq (mRNA) | n/a | n/a | |||||||||||
RefSeq (protein) | n/a | n/a | |||||||||||
Location (UCSC) | n/a | n/a | |||||||||||
PubMed search | n/a | n/a |
Mitogen-activated protein kinase-activated protein kinase 2, also known as MAPKAPK2, is a human gene.
This gene encodes a member of the Ser/Thr protein kinase family. This kinase is regulated through direct phosphorylation by p38 MAP kinase. In conjunction with p38 MAP kinase, this kinase is known to be involved in many cellular processes including stress and inflammatory responses, nuclear export, gene expression regulation and cell proliferation. Heat shock protein HSP27 was shown to be one of the substrates of this kinase in vivo. Two transcript variants encoding two different isoforms have been found for this gene.[1]
References
Further reading
- Ben-Levy R, Hooper S, Wilson R; et al. (1999). "Nuclear export of the stress-activated protein kinase p38 mediated by its substrate MAPKAP kinase-2". Curr. Biol. 8 (19): 1049–57. PMID 9768359.
- Stokoe D, Engel K, Campbell DG; et al. (1992). "Identification of MAPKAP kinase 2 as a major enzyme responsible for the phosphorylation of the small mammalian heat shock proteins". FEBS Lett. 313 (3): 307–13. PMID 1332886.
- Vulliet PR, Woodgett JR, Cohen P (1984). "Phosphorylation of tyrosine hydroxylase by calmodulin-dependent multiprotein kinase". J. Biol. Chem. 259 (22): 13680–3. PMID 6150037.
- Engel K, Schultz H, Martin F; et al. (1995). "Constitutive activation of mitogen-activated protein kinase-activated protein kinase 2 by mutation of phosphorylation sites and an A-helix motif". J. Biol. Chem. 270 (45): 27213–21. PMID 7592979.
- Lavoie JN, Lambert H, Hickey E; et al. (1995). "Modulation of cellular thermoresistance and actin filament stability accompanies phosphorylation-induced changes in the oligomeric structure of heat shock protein 27". Mol. Cell. Biol. 15 (1): 505–16. PMID 7799959.
- Sutherland C, Alterio J, Campbell DG; et al. (1993). "Phosphorylation and activation of human tyrosine hydroxylase in vitro by mitogen-activated protein (MAP) kinase and MAP-kinase-activated kinases 1 and 2". Eur. J. Biochem. 217 (2): 715–22. PMID 7901013.
- Knauf U, Jakob U, Engel K; et al. (1994). "Stress- and mitogen-induced phosphorylation of the small heat shock protein Hsp25 by MAPKAP kinase 2 is not essential for chaperone properties and cellular thermoresistance". EMBO J. 13 (1): 54–60. PMID 7905823.
- Freshney NW, Rawlinson L, Guesdon F; et al. (1994). "Interleukin-1 activates a novel protein kinase cascade that results in the phosphorylation of Hsp27". Cell. 78 (6): 1039–49. PMID 7923354.
- Zu YL, Wu F, Gilchrist A; et al. (1994). "The primary structure of a human MAP kinase activated protein kinase 2". Biochem. Biophys. Res. Commun. 200 (2): 1118–24. PMID 8179591.
- Stokoe D, Caudwell B, Cohen PT, Cohen P (1994). "The substrate specificity and structure of mitogen-activated protein (MAP) kinase-activated protein kinase-2". Biochem. J. 296 ( Pt 3): 843–9. PMID 8280084.
- Rivera VM, Miranti CK, Misra RP; et al. (1993). "A growth factor-induced kinase phosphorylates the serum response factor at a site that regulates its DNA-binding activity". Mol. Cell. Biol. 13 (10): 6260–73. PMID 8413226.
- Beyaert R, Cuenda A, Vanden Berghe W; et al. (1996). "The p38/RK mitogen-activated protein kinase pathway regulates interleukin-6 synthesis response to tumor necrosis factor". EMBO J. 15 (8): 1914–23. PMID 8617238.
- Ben-Levy R, Leighton IA, Doza YN; et al. (1996). "Identification of novel phosphorylation sites required for activation of MAPKAP kinase-2". EMBO J. 14 (23): 5920–30. PMID 8846784.
- Tan Y, Rouse J, Zhang A; et al. (1997). "FGF and stress regulate CREB and ATF-1 via a pathway involving p38 MAP kinase and MAPKAP kinase-2". EMBO J. 15 (17): 4629–42. PMID 8887554.
- Huang CK, Zhan L, Ai Y, Jongstra J (1997). "LSP1 is the major substrate for mitogen-activated protein kinase-activated protein kinase 2 in human neutrophils". J. Biol. Chem. 272 (1): 17–9. PMID 8995217.
- Krump E, Sanghera JS, Pelech SL; et al. (1997). "Chemotactic peptide N-formyl-met-leu-phe activation of p38 mitogen-activated protein kinase (MAPK) and MAPK-activated protein kinase-2 in human neutrophils". J. Biol. Chem. 272 (2): 937–44. PMID 8995385.
- Engel K, Kotlyarov A, Gaestel M (1998). "Leptomycin B-sensitive nuclear export of MAPKAP kinase 2 is regulated by phosphorylation". EMBO J. 17 (12): 3363–71. doi:10.1093/emboj/17.12.3363. PMID 9628873.
- Craxton A, Shu G, Graves JD; et al. (1998). "p38 MAPK is required for CD40-induced gene expression and proliferation in B lymphocytes". J. Immunol. 161 (7): 3225–36. PMID 9759836.
- Heidenreich O, Neininger A, Schratt G; et al. (1999). "MAPKAP kinase 2 phosphorylates serum response factor in vitro and in vivo". J. Biol. Chem. 274 (20): 14434–43. PMID 10318869.
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