MAPKAPK2

Mitogen-activated protein kinase-activated protein kinase 2, also known as MAPKAPK2, is a human gene.

PBB_Summary
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summary_text = 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.cite web | title = Entrez Gene: MAPKAPK2 mitogen-activated protein kinase-activated protein kinase 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9261| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Ben-Levy R, Hooper S, Wilson R, "et al." |title=Nuclear export of the stress-activated protein kinase p38 mediated by its substrate MAPKAP kinase-2. |journal=Curr. Biol. |volume=8 |issue= 19 |pages= 1049–57 |year= 1999 |pmid= 9768359 |doi=
*cite journal | author=Stokoe D, Engel K, Campbell DG, "et al." |title=Identification of MAPKAP kinase 2 as a major enzyme responsible for the phosphorylation of the small mammalian heat shock proteins. |journal=FEBS Lett. |volume=313 |issue= 3 |pages= 307–13 |year= 1992 |pmid= 1332886 |doi=
*cite journal | author=Vulliet PR, Woodgett JR, Cohen P |title=Phosphorylation of tyrosine hydroxylase by calmodulin-dependent multiprotein kinase. |journal=J. Biol. Chem. |volume=259 |issue= 22 |pages= 13680–3 |year= 1984 |pmid= 6150037 |doi=
*cite journal | author=Engel K, Schultz H, Martin F, "et al." |title=Constitutive activation of mitogen-activated protein kinase-activated protein kinase 2 by mutation of phosphorylation sites and an A-helix motif. |journal=J. Biol. Chem. |volume=270 |issue= 45 |pages= 27213–21 |year= 1995 |pmid= 7592979 |doi=
*cite journal | author=Lavoie JN, Lambert H, Hickey E, "et al." |title=Modulation of cellular thermoresistance and actin filament stability accompanies phosphorylation-induced changes in the oligomeric structure of heat shock protein 27. |journal=Mol. Cell. Biol. |volume=15 |issue= 1 |pages= 505–16 |year= 1995 |pmid= 7799959 |doi=
*cite journal | author=Sutherland C, Alterio J, Campbell DG, "et al." |title=Phosphorylation and activation of human tyrosine hydroxylase in vitro by mitogen-activated protein (MAP) kinase and MAP-kinase-activated kinases 1 and 2. |journal=Eur. J. Biochem. |volume=217 |issue= 2 |pages= 715–22 |year= 1993 |pmid= 7901013 |doi=
*cite journal | author=Knauf U, Jakob U, Engel K, "et al." |title=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. |journal=EMBO J. |volume=13 |issue= 1 |pages= 54–60 |year= 1994 |pmid= 7905823 |doi=
*cite journal | author=Freshney NW, Rawlinson L, Guesdon F, "et al." |title=Interleukin-1 activates a novel protein kinase cascade that results in the phosphorylation of Hsp27. |journal=Cell |volume=78 |issue= 6 |pages= 1039–49 |year= 1994 |pmid= 7923354 |doi=
*cite journal | author=Zu YL, Wu F, Gilchrist A, "et al." |title=The primary structure of a human MAP kinase activated protein kinase 2. |journal=Biochem. Biophys. Res. Commun. |volume=200 |issue= 2 |pages= 1118–24 |year= 1994 |pmid= 8179591 |doi=
*cite journal | author=Stokoe D, Caudwell B, Cohen PT, Cohen P |title=The substrate specificity and structure of mitogen-activated protein (MAP) kinase-activated protein kinase-2. |journal=Biochem. J. |volume=296 ( Pt 3) |issue= |pages= 843–9 |year= 1994 |pmid= 8280084 |doi=
*cite journal | author=Rivera VM, Miranti CK, Misra RP, "et al." |title=A growth factor-induced kinase phosphorylates the serum response factor at a site that regulates its DNA-binding activity. |journal=Mol. Cell. Biol. |volume=13 |issue= 10 |pages= 6260–73 |year= 1993 |pmid= 8413226 |doi=
*cite journal | author=Beyaert R, Cuenda A, Vanden Berghe W, "et al." |title=The p38/RK mitogen-activated protein kinase pathway regulates interleukin-6 synthesis response to tumor necrosis factor. |journal=EMBO J. |volume=15 |issue= 8 |pages= 1914–23 |year= 1996 |pmid= 8617238 |doi=
*cite journal | author=Ben-Levy R, Leighton IA, Doza YN, "et al." |title=Identification of novel phosphorylation sites required for activation of MAPKAP kinase-2. |journal=EMBO J. |volume=14 |issue= 23 |pages= 5920–30 |year= 1996 |pmid= 8846784 |doi=
*cite journal | author=Tan Y, Rouse J, Zhang A, "et al." |title=FGF and stress regulate CREB and ATF-1 via a pathway involving p38 MAP kinase and MAPKAP kinase-2. |journal=EMBO J. |volume=15 |issue= 17 |pages= 4629–42 |year= 1997 |pmid= 8887554 |doi=
*cite journal | author=Huang CK, Zhan L, Ai Y, Jongstra J |title=LSP1 is the major substrate for mitogen-activated protein kinase-activated protein kinase 2 in human neutrophils. |journal=J. Biol. Chem. |volume=272 |issue= 1 |pages= 17–9 |year= 1997 |pmid= 8995217 |doi=
*cite journal | author=Krump E, Sanghera JS, Pelech SL, "et al." |title=Chemotactic peptide N-formyl-met-leu-phe activation of p38 mitogen-activated protein kinase (MAPK) and MAPK-activated protein kinase-2 in human neutrophils. |journal=J. Biol. Chem. |volume=272 |issue= 2 |pages= 937–44 |year= 1997 |pmid= 8995385 |doi=
*cite journal | author=Engel K, Kotlyarov A, Gaestel M |title=Leptomycin B-sensitive nuclear export of MAPKAP kinase 2 is regulated by phosphorylation. |journal=EMBO J. |volume=17 |issue= 12 |pages= 3363–71 |year= 1998 |pmid= 9628873 |doi= 10.1093/emboj/17.12.3363
*cite journal | author=Craxton A, Shu G, Graves JD, "et al." |title=p38 MAPK is required for CD40-induced gene expression and proliferation in B lymphocytes. |journal=J. Immunol. |volume=161 |issue= 7 |pages= 3225–36 |year= 1998 |pmid= 9759836 |doi=
*cite journal | author=Heidenreich O, Neininger A, Schratt G, "et al." |title=MAPKAP kinase 2 phosphorylates serum response factor in vitro and in vivo. |journal=J. Biol. Chem. |volume=274 |issue= 20 |pages= 14434–43 |year= 1999 |pmid= 10318869 |doi=

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