MAP2K2

MAP2K2

Mitogen-activated protein kinase kinase 2, also known as MAP2K2, is a human gene.

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summary_text = The protein encoded by this gene is a dual specificity protein kinase that belongs to the MAP kinase kinase family. This kinase is known to play a critical role in mitogen growth factor signal transduction. It phosphorylates and thus activates MAPK1/ERK2 and MAPK2/ERK3. The activation of this kinase itself is dependent on the Ser/Thr phosphorylation by MAP kinase kinase kinases. The inhibition or degradation of this kinase is found to be involved in the pathogenesis of Yersinia and anthrax. [cite web | title = Entrez Gene: MAP2K2 mitogen-activated protein kinase kinase 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5605| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Joseph AM, Kumar M, Mitra D |title=Nef: "necessary and enforcing factor" in HIV infection. |journal=Curr. HIV Res. |volume=3 |issue= 1 |pages= 87–94 |year= 2005 |pmid= 15638726 |doi=
*cite journal | author=Stove V, Verhasselt B |title=Modelling thymic HIV-1 Nef effects. |journal=Curr. HIV Res. |volume=4 |issue= 1 |pages= 57–64 |year= 2006 |pmid= 16454711 |doi=
*cite journal | author=Charest DL, Mordret G, Harder KW, "et al." |title=Molecular cloning, expression, and characterization of the human mitogen-activated protein kinase p44erk1. |journal=Mol. Cell. Biol. |volume=13 |issue= 8 |pages= 4679–90 |year= 1993 |pmid= 7687743 |doi=
*cite journal | author=Dérijard B, Raingeaud J, Barrett T, "et al." |title=Independent human MAP-kinase signal transduction pathways defined by MEK and MKK isoforms. |journal=Science |volume=267 |issue= 5198 |pages= 682–5 |year= 1995 |pmid= 7839144 |doi=
*cite journal | author=Alessi DR, Saito Y, Campbell DG, "et al." |title=Identification of the sites in MAP kinase kinase-1 phosphorylated by p74raf-1. |journal=EMBO J. |volume=13 |issue= 7 |pages= 1610–9 |year= 1994 |pmid= 8157000 |doi=
*cite journal | author=Zheng CF, Guan KL |title=Properties of MEKs, the kinases that phosphorylate and activate the extracellular signal-regulated kinases. |journal=J. Biol. Chem. |volume=268 |issue= 32 |pages= 23933–9 |year= 1993 |pmid= 8226933 |doi=
*cite journal | author=Zheng CF, Guan KL |title=Cloning and characterization of two distinct human extracellular signal-regulated kinase activator kinases, MEK1 and MEK2. |journal=J. Biol. Chem. |volume=268 |issue= 15 |pages= 11435–9 |year= 1993 |pmid= 8388392 |doi=
*cite journal | author=Wu J, Harrison JK, Dent P, "et al." |title=Identification and characterization of a new mammalian mitogen-activated protein kinase kinase, MKK2. |journal=Mol. Cell. Biol. |volume=13 |issue= 8 |pages= 4539–48 |year= 1993 |pmid= 8393135 |doi=
*cite journal | author=Moriguchi T, Gotoh Y, Nishida E |title=Activation of two isoforms of mitogen-activated protein kinase kinase in response to epidermal growth factor and nerve growth factor. |journal=Eur. J. Biochem. |volume=234 |issue= 1 |pages= 32–8 |year= 1996 |pmid= 8529659 |doi=
*cite journal | author=Butch ER, Guan KL |title=Characterization of ERK1 activation site mutants and the effect on recognition by MEK1 and MEK2. |journal=J. Biol. Chem. |volume=271 |issue= 8 |pages= 4230–5 |year= 1996 |pmid= 8626767 |doi=
*cite journal | author=Papin C, Denouel A, Calothy G, Eychène A |title=Identification of signalling proteins interacting with B-Raf in the yeast two-hybrid system. |journal=Oncogene |volume=12 |issue= 10 |pages= 2213–21 |year= 1996 |pmid= 8668348 |doi=
*cite journal | author=Downey GP, Butler JR, Brumell J, "et al." |title=Chemotactic peptide-induced activation of MEK-2, the predominant isoform in human neutrophils. Inhibition by wortmannin. |journal=J. Biol. Chem. |volume=271 |issue= 35 |pages= 21005–1011 |year= 1996 |pmid= 8702863 |doi=
*cite journal | author=Khoo S, Cobb MH |title=Activation of mitogen-activating protein kinase by glucose is not required for insulin secretion. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 11 |pages= 5599–604 |year= 1997 |pmid= 9159118 |doi=
*cite journal | author=Li CJ, Ueda Y, Shi B, "et al." |title=Tat protein induces self-perpetuating permissivity for productive HIV-1 infection. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 15 |pages= 8116–20 |year= 1997 |pmid= 9223324 |doi=
*cite journal | author=Menegon A, Leoni C, Benfenati F, Valtorta F |title=Tat protein from HIV-1 activates MAP kinase in granular neurons and glial cells from rat cerebellum. |journal=Biochem. Biophys. Res. Commun. |volume=238 |issue= 3 |pages= 800–5 |year= 1997 |pmid= 9325171 |doi= 10.1006/bbrc.1997.7393
*cite journal | author=Denouel-Galy A, Douville EM, Warne PH, "et al." |title=Murine Ksr interacts with MEK and inhibits Ras-induced transformation. |journal=Curr. Biol. |volume=8 |issue= 1 |pages= 46–55 |year= 1998 |pmid= 9427625 |doi=
*cite journal | author=Gibellini D, Bassini A, Pierpaoli S, "et al." |title=Extracellular HIV-1 Tat protein induces the rapid Ser133 phosphorylation and activation of CREB transcription factor in both Jurkat lymphoblastoid T cells and primary peripheral blood mononuclear cells. |journal=J. Immunol. |volume=160 |issue= 8 |pages= 3891–8 |year= 1998 |pmid= 9558095 |doi=
*cite journal | author=Duesbery NS, Webb CP, Leppla SH, "et al." |title=Proteolytic inactivation of MAP-kinase-kinase by anthrax lethal factor. |journal=Science |volume=280 |issue= 5364 |pages= 734–7 |year= 1998 |pmid= 9563949 |doi=
*cite journal | author=Ganju RK, Munshi N, Nair BC, "et al." |title=Human immunodeficiency virus tat modulates the Flk-1/KDR receptor, mitogen-activated protein kinases, and components of focal adhesion in Kaposi's sarcoma cells. |journal=J. Virol. |volume=72 |issue= 7 |pages= 6131–7 |year= 1998 |pmid= 9621077 |doi=
*cite journal | author=Tanimura S, Chatani Y, Hoshino R, "et al." |title=Activation of the 41/43 kDa mitogen-activated protein kinase signaling pathway is required for hepatocyte growth factor-induced cell scattering. |journal=Oncogene |volume=17 |issue= 1 |pages= 57–65 |year= 1998 |pmid= 9671314 |doi= 10.1038/sj.onc.1201905

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