| 释义 |
- Function
- Interactions
- References
- Further reading
- External links
{{main|Mitogen-activated protein kinase}}{{Infobox_gene}}Mitogen-activated protein kinase 7 also known as MAP kinase 7 is an enzyme that in humans is encoded by the MAPK7 gene.[1][2] Function MAPK7 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 specifically activated by mitogen-activated protein kinase kinase 5 (MAP2K5/MEK5). It is involved in the downstream signaling processes of various receptor molecules including receptor tyrosine kinases, and G protein-coupled receptors. In response to extracellular signals, this kinase translocates to the cell nucleus, where it regulates gene expression by phosphorylating, and activating different transcription factors. Four alternatively spliced transcript variants of this gene encoding two distinct isoforms have been reported.[3] MAPK7 is also critical for cardiovascular development [4] and is essential for endothelial cell function.[5][6] Interactions MAPK7 has been shown to interact with: {{div col|colwidth=20em}}- C-Raf,[7]
- Gap junction protein, alpha 1[8]
- MAP2K5,[2]
- MEF2C,[9]
- MEF2D,[9]
- PTPRR,[10]
- SGK,[11] and
- YWHAB.[12]
{{Div col end}} References 1. ^{{cite journal | vauthors = Purandare SM, Lee JD, Patel PI | title = Assignment of big MAP kinase (PRKM7) to human chromosome 17 band p11.2 with somatic cell hybrids | journal = Cytogenet. Cell Genet. | volume = 83 | issue = 3–4 | pages = 258–9 | date = March 1999 | pmid = 10072598 | pmc = | doi = 10.1159/000015199 }}
2. ^1 {{cite journal | vauthors = Zhou G, Bao ZQ, Dixon JE | title = Components of a new human protein kinase signal transduction pathway | journal = J. Biol. Chem. | volume = 270 | issue = 21 | pages = 12665–9 | date = Jun 1995 | pmid = 7759517 | pmc = | doi = 10.1074/jbc.270.21.12665 }}
3. ^{{cite web | title = Entrez Gene: MAPK7 mitogen-activated protein kinase 7| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5598| accessdate = }}
4. ^{{cite journal | vauthors = Hayashi M, Lee JD | title = Role of the BMK1/ERK5 signaling pathway: lessons from knockout mice | journal = J. Mol. Med. | volume = 82 | issue = 12 | pages = 800–8 | date = Oct 2004 | pmid = 15517128 | pmc = | doi = 10.1007/s00109-004-0602-8 }}
5. ^{{cite journal | vauthors = Roberts OL, Holmes K, Müller J, Cross DA, Cross MJ | title = ERK5 and the regulation of endothelial cell function | journal = Biochem. Soc. Trans. | volume = 37 | issue = Pt 6 | pages = 1254–9 | date = Dec 2009 | pmid = 19909257 | pmc = | doi = 10.1042/BST0371254 }}
6. ^{{cite journal | vauthors = Roberts OL, Holmes K, Müller J, Cross DA, Cross MJ | title = ERK5 is required for VEGF-mediated survival and tubular morphogenesis of primary human microvascular endothelial cells | journal = J. Cell Sci. | volume = 123 | issue = Pt 18 | pages = 3189–200 | date = Sep 2010 | pmid = 20736307 | pmc = | doi = 10.1242/jcs.072801 }}
7. ^{{cite journal | vauthors = English JM, Pearson G, Hockenberry T, Shivakumar L, White MA, Cobb MH | title = Contribution of the ERK5/MEK5 pathway to Ras/Raf signaling and growth control | journal = J. Biol. Chem. | volume = 274 | issue = 44 | pages = 31588–92 | date = Oct 1999 | pmid = 10531364 | doi = 10.1074/jbc.274.44.31588}}
8. ^{{cite journal | vauthors = Cameron SJ, Malik S, Akaike M, Lerner-Marmarosh N, Yan C, Lee JD, Abe J, Yang J | title = Regulation of epidermal growth factor-induced connexin 43 gap junction communication by big mitogen-activated protein kinase1/ERK5 but not ERK1/2 kinase activation | journal = J. Biol. Chem. | volume = 278 | issue = 20 | pages = 18682–8 | date = May 2003 | pmid = 12637502 | doi = 10.1074/jbc.M213283200 }}
9. ^1 {{cite journal | vauthors = Yang CC, Ornatsky OI, McDermott JC, Cruz TF, Prody CA | title = Interaction of myocyte enhancer factor 2 (MEF2) with a mitogen-activated protein kinase, ERK5/BMK1 | journal = Nucleic Acids Res. | volume = 26 | issue = 20 | pages = 4771–7 | date = Oct 1998 | pmid = 9753748 | pmc = 147902 | doi = 10.1093/nar/26.20.4771}}
10. ^{{cite journal | vauthors = Buschbeck M, Eickhoff J, Sommer MN, Ullrich A | title = Phosphotyrosine-specific phosphatase PTP-SL regulates the ERK5 signaling pathway | journal = J. Biol. Chem. | volume = 277 | issue = 33 | pages = 29503–9 | date = Aug 2002 | pmid = 12042304 | doi = 10.1074/jbc.M202149200 }}
11. ^{{cite journal | vauthors = Hayashi M, Tapping RI, Chao TH, Lo JF, King CC, Yang Y, Lee JD | title = BMK1 mediates growth factor-induced cell proliferation through direct cellular activation of serum and glucocorticoid-inducible kinase | journal = J. Biol. Chem. | volume = 276 | issue = 12 | pages = 8631–4 | date = Mar 2001 | pmid = 11254654 | doi = 10.1074/jbc.C000838200 }}
12. ^{{cite journal | vauthors = Zheng Q, Yin G, Yan C, Cavet M, Berk BC | title = 14-3-3beta binds to big mitogen-activated protein kinase 1 (BMK1/ERK5) and regulates BMK1 function | journal = J. Biol. Chem. | volume = 279 | issue = 10 | pages = 8787–91 | date = Mar 2004 | pmid = 14679215 | doi = 10.1074/jbc.M310212200 }}
Further reading {{refbegin | 2}}- {{cite journal | vauthors = Lee JD, Ulevitch RJ, Han J | title = Primary structure of BMK1: a new mammalian map kinase | journal = Biochem. Biophys. Res. Commun. | volume = 213 | issue = 2 | pages = 715–24 | year = 1995 | pmid = 7646528 | doi = 10.1006/bbrc.1995.2189 }}
- {{cite journal | vauthors = Warn-Cramer BJ, Lampe PD, Kurata WE, Kanemitsu MY, Loo LW, Eckhart W, Lau AF | title = Characterization of the mitogen-activated protein kinase phosphorylation sites on the connexin-43 gap junction protein | journal = J. Biol. Chem. | volume = 271 | issue = 7 | pages = 3779–86 | year = 1996 | pmid = 8631994 | doi = 10.1074/jbc.271.7.3779 }}
- {{cite journal | vauthors = Kato Y, Kravchenko VV, Tapping RI, Han J, Ulevitch RJ, Lee JD | title = BMK1/ERK5 regulates serum-induced early gene expression through transcription factor MEF2C | journal = EMBO J. | volume = 16 | issue = 23 | pages = 7054–66 | year = 1997 | pmid = 9384584 | pmc = 1170308 | doi = 10.1093/emboj/16.23.7054 }}
- {{cite journal | vauthors = English JM, Pearson G, Baer R, Cobb MH | title = Identification of substrates and regulators of the mitogen-activated protein kinase ERK5 using chimeric protein kinases | journal = J. Biol. Chem. | volume = 273 | issue = 7 | pages = 3854–60 | year = 1998 | pmid = 9461566 | doi = 10.1074/jbc.273.7.3854 }}
- {{cite journal | vauthors = Grunwald ME, Yu WP, Yu HH, Yau KW | title = Identification of a domain on the beta-subunit of the rod cGMP-gated cation channel that mediates inhibition by calcium-calmodulin | journal = J. Biol. Chem. | volume = 273 | issue = 15 | pages = 9148–57 | year = 1998 | pmid = 9535905 | doi = 10.1074/jbc.273.15.9148 }}
- {{cite journal | vauthors = Warn-Cramer BJ, Cottrell GT, Burt JM, Lau AF | title = Regulation of connexin-43 gap junctional intercellular communication by mitogen-activated protein kinase | journal = J. Biol. Chem. | volume = 273 | issue = 15 | pages = 9188–96 | year = 1998 | pmid = 9535909 | doi = 10.1074/jbc.273.15.9188 }}
- {{cite journal | vauthors = Yang CC, Ornatsky OI, McDermott JC, Cruz TF, Prody CA | title = Interaction of myocyte enhancer factor 2 (MEF2) with a mitogen-activated protein kinase, ERK5/BMK1 | journal = Nucleic Acids Res. | volume = 26 | issue = 20 | pages = 4771–7 | year = 1998 | pmid = 9753748 | pmc = 147902 | doi = 10.1093/nar/26.20.4771 }}
- {{cite journal | vauthors = Kato Y, Tapping RI, Huang S, Watson MH, Ulevitch RJ, Lee JD | title = Bmk1/Erk5 is required for cell proliferation induced by epidermal growth factor | journal = Nature | volume = 395 | issue = 6703 | pages = 713–6 | year = 1998 | pmid = 9790194 | doi = 10.1038/27234 }}
- {{cite journal | vauthors = Zhao M, New L, Kravchenko VV, Kato Y, Gram H, di Padova F, Olson EN, Ulevitch RJ, Han J | title = Regulation of the MEF2 family of transcription factors by p38 | journal = Mol. Cell. Biol. | volume = 19 | issue = 1 | pages = 21–30 | year = 1999 | pmid = 9858528 | pmc = 83862 | doi = 10.1128/mcb.19.1.21}}
- {{cite journal | vauthors = Kamakura S, Moriguchi T, Nishida E | title = Activation of the protein kinase ERK5/BMK1 by receptor tyrosine kinases. Identification and characterization of a signaling pathway to the nucleus | journal = J. Biol. Chem. | volume = 274 | issue = 37 | pages = 26563–71 | year = 1999 | pmid = 10473620 | doi = 10.1074/jbc.274.37.26563 }}
- {{cite journal | vauthors = English JM, Pearson G, Hockenberry T, Shivakumar L, White MA, Cobb MH | title = Contribution of the ERK5/MEK5 pathway to Ras/Raf signaling and growth control | journal = J. Biol. Chem. | volume = 274 | issue = 44 | pages = 31588–92 | year = 1999 | pmid = 10531364 | doi = 10.1074/jbc.274.44.31588 }}
- {{cite journal | vauthors = Fukuhara S, Marinissen MJ, Chiariello M, Gutkind JS | title = Signaling from G protein-coupled receptors to ERK5/Big MAPK 1 involves Galpha q and Galpha 12/13 families of heterotrimeric G proteins. Evidence for the existence of a novel Ras AND Rho-independent pathway | journal = J. Biol. Chem. | volume = 275 | issue = 28 | pages = 21730–6 | year = 2000 | pmid = 10781600 | doi = 10.1074/jbc.M002410200 }}
- {{cite journal | vauthors = Kato Y, Zhao M, Morikawa A, Sugiyama T, Chakravortty D, Koide N, Yoshida T, Tapping RI, Yang Y, Yokochi T, Lee JD | title = Big mitogen-activated kinase regulates multiple members of the MEF2 protein family | journal = J. Biol. Chem. | volume = 275 | issue = 24 | pages = 18534–40 | year = 2000 | pmid = 10849446 | doi = 10.1074/jbc.M001573200 }}
- {{cite journal | vauthors = Yan C, Luo H, Lee JD, Abe J, Berk BC | title = Molecular cloning of mouse ERK5/BMK1 splice variants and characterization of ERK5 functional domains | journal = J. Biol. Chem. | volume = 276 | issue = 14 | pages = 10870–8 | year = 2001 | pmid = 11139578 | doi = 10.1074/jbc.M009286200 }}
- {{cite journal | vauthors = Hayashi M, Tapping RI, Chao TH, Lo JF, King CC, Yang Y, Lee JD | title = BMK1 mediates growth factor-induced cell proliferation through direct cellular activation of serum and glucocorticoid-inducible kinase | journal = J. Biol. Chem. | volume = 276 | issue = 12 | pages = 8631–4 | year = 2001 | pmid = 11254654 | doi = 10.1074/jbc.C000838200 }}
- {{cite journal | vauthors = Dong F, Gutkind JS, Larner AC | title = Granulocyte colony-stimulating factor induces ERK5 activation, which is differentially regulated by protein-tyrosine kinases and protein kinase C. Regulation of cell proliferation and survival | journal = J. Biol. Chem. | volume = 276 | issue = 14 | pages = 10811–6 | year = 2001 | pmid = 11278431 | doi = 10.1074/jbc.M008748200 }}
- {{cite journal | vauthors = Watson FL, Heerssen HM, Bhattacharyya A, Klesse L, Lin MZ, Segal RA | title = Neurotrophins use the Erk5 pathway to mediate a retrograde survival response | journal = Nat. Neurosci. | volume = 4 | issue = 10 | pages = 981–8 | year = 2001 | pmid = 11544482 | doi = 10.1038/nn720 }}
- {{cite journal | vauthors = Esparís-Ogando A, Díaz-Rodríguez E, Montero JC, Yuste L, Crespo P, Pandiella A | title = Erk5 participates in neuregulin signal transduction and is constitutively active in breast cancer cells overexpressing ErbB2 | journal = Mol. Cell. Biol. | volume = 22 | issue = 1 | pages = 270–85 | year = 2002 | pmid = 11739740 | pmc = 134212 | doi = 10.1128/MCB.22.1.270-285.2002 }}
{{refend}} External links {{Serine/threonine-specific protein kinases}}{{Enzymes}}{{Portal bar|Molecular and Cellular Biology|border=no}} 1 : EC 2.7.11 |