词条 | MAP3K7 |
释义 |
FunctionThe protein encoded by this gene is a member of the serine/threonine protein kinase family. This kinase mediates the signaling transduction induced by TGF beta and morphogenetic protein (BMP), and controls a variety of cell functions including transcription regulation and apoptosis. TAK1 is a central regulator of cell death and is activated through a diverse set of intra- and extracellular stimuli. TAK1 regulates cell survival not solely through NF-κB but also through NF-κB-independent pathways such as oxidative stress and receptor-interacting protein kinase 1 (RIPK1) kinase activity-dependent pathway.[2] In response to IL-1, this protein forms a kinase complex including TRAF6, MAP3K7P1/TAB1 and MAP3K7P2/TAB2; this complex is required for the activation of nuclear factor kappa B. This kinase can also activate MAPK8/JNK, MAP2K4/MKK4, and thus plays a role in the cell response to environmental stresses. Four alternatively spliced transcript variants encoding distinct isoforms have been reported.[3] InteractionsMAP3K7 has been shown to interact with: {{div col|colwidth=20em}}
References1. ^{{cite journal | vauthors = Kondo M, Osada H, Uchida K, Yanagisawa K, Masuda A, Takagi K, Takahashi T, Takahashi T | title = Molecular cloning of human TAK1 and its mutational analysis in human lung cancer | journal = Int J Cancer | volume = 75 | issue = 4 | pages = 559–63 | date = February 1998 | pmid = 9466656 | pmc = | doi = 10.1002/(SICI)1097-0215(19980209)75:4<559::AID-IJC11>3.0.CO;2-4 }} 2. ^{{Cite journal|last=Mihaly|first=S. R.|last2=Ninomiya-Tsuji|first2=J.|last3=Morioka|first3=S.|date=2014-11-01|title=TAK1 control of cell death|url=http://www.nature.com/cdd/journal/v21/n11/full/cdd2014123a.html|journal=Cell Death & Differentiation|language=en|volume=21|issue=11|pages=1667–1676|doi=10.1038/cdd.2014.123|issn=1350-9047|pmc=4211365|pmid=25146924}} 3. ^{{cite web | title = Entrez Gene: MAP3K7 mitogen-activated protein kinase kinase kinase 7| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6885| accessdate = }} 4. ^1 {{cite journal | vauthors = Mochida Y, Takeda K, Saitoh M, Nishitoh H, Amagasa T, Ninomiya-Tsuji J, Matsumoto K, Ichijo H | title = ASK1 inhibits interleukin-1-induced NF-kappa B activity through disruption of TRAF6-TAK1 interaction | journal = J. Biol. Chem. | volume = 275 | issue = 42 | pages = 32747–52 | date = October 2000 | pmid = 10921914 | doi = 10.1074/jbc.M003042200 }} 5. ^{{cite journal | vauthors = Sakurai H, Miyoshi H, Toriumi W, Sugita T | title = Functional interactions of transforming growth factor beta-activated kinase 1 with IkappaB kinases to stimulate NF-kappaB activation | journal = J. Biol. Chem. | volume = 274 | issue = 15 | pages = 10641–8 | date = April 1999 | pmid = 10187861 | doi = 10.1074/jbc.274.15.10641}} 6. ^{{cite journal | vauthors = Wang C, Deng L, Hong M, Akkaraju GR, Inoue J, Chen ZJ | title = TAK1 is a ubiquitin-dependent kinase of MKK and IKK | journal = Nature | volume = 412 | issue = 6844 | pages = 346–51 | date = July 2001 | pmid = 11460167 | doi = 10.1038/35085597 }} 7. ^1 2 3 {{cite journal | vauthors = Ninomiya-Tsuji J, Kishimoto K, Hiyama A, Inoue J, Cao Z, Matsumoto K | title = The kinase TAK1 can activate the NIK-I kappaB as well as the MAP kinase cascade in the IL-1 signalling pathway | journal = Nature | volume = 398 | issue = 6724 | pages = 252–6 | date = March 1999 | pmid = 10094049 | doi = 10.1038/18465 }} 8. ^1 {{cite journal | vauthors = Sakurai H, Miyoshi H, Mizukami J, Sugita T | title = Phosphorylation-dependent activation of TAK1 mitogen-activated protein kinase kinase kinase by TAB1 | journal = FEBS Lett. | volume = 474 | issue = 2–3 | pages = 141–5 | date = June 2000 | pmid = 10838074 | doi = 10.1016/s0014-5793(00)01588-x}} 9. ^{{cite journal | vauthors = Channavajhala PL, Wu L, Cuozzo JW, Hall JP, Liu W, Lin LL, Zhang Y | title = Identification of a novel human kinase supporter of Ras (hKSR-2) that functions as a negative regulator of Cot (Tpl2) signaling | journal = J. Biol. Chem. | volume = 278 | issue = 47 | pages = 47089–97 | date = November 2003 | pmid = 12975377 | doi = 10.1074/jbc.M306002200 }} 10. ^1 2 {{cite journal | vauthors = Cheung PC, Nebreda AR, Cohen P | title = TAB3, a new binding partner of the protein kinase TAK1 | journal = Biochem. J. | volume = 378 | issue = Pt 1 | pages = 27–34 | date = February 2004 | pmid = 14670075 | pmc = 1223947 | doi = 10.1042/BJ20031794 }} 11. ^1 {{cite journal | vauthors = Takaesu G, Kishida S, Hiyama A, Yamaguchi K, Shibuya H, Irie K, Ninomiya-Tsuji J, Matsumoto K | title = TAB2, a novel adaptor protein, mediates activation of TAK1 MAPKKK by linking TAK1 to TRAF6 in the IL-1 signal transduction pathway | journal = Mol. Cell | volume = 5 | issue = 4 | pages = 649–58 | date = April 2000 | pmid = 10882101 | doi = 10.1016/s1097-2765(00)80244-0}} 12. ^1 {{cite journal | vauthors = Takaesu G, Ninomiya-Tsuji J, Kishida S, Li X, Stark GR, Matsumoto K | title = Interleukin-1 (IL-1) receptor-associated kinase leads to activation of TAK1 by inducing TAB2 translocation in the IL-1 signaling pathway | journal = Mol. Cell. Biol. | volume = 21 | issue = 7 | pages = 2475–84 | date = April 2001 | pmid = 11259596 | pmc = 86880 | doi = 10.1128/MCB.21.7.2475-2484.2001 }} 13. ^1 2 {{cite journal | vauthors = Ishitani T, Takaesu G, Ninomiya-Tsuji J, Shibuya H, Gaynor RB, Matsumoto K | title = Role of the TAB2-related protein TAB3 in IL-1 and TNF signaling | journal = EMBO J. | volume = 22 | issue = 23 | pages = 6277–88 | date = December 2003 | pmid = 14633987 | pmc = 291846 | doi = 10.1093/emboj/cdg605 }} 14. ^{{cite journal | vauthors = Kimura N, Matsuo R, Shibuya H, Nakashima K, Taga T | title = BMP2-induced apoptosis is mediated by activation of the TAK1-p38 kinase pathway that is negatively regulated by Smad6 | journal = J. Biol. Chem. | volume = 275 | issue = 23 | pages = 17647–52 | date = June 2000 | pmid = 10748100 | doi = 10.1074/jbc.M908622199 }} 15. ^{{cite journal | vauthors = Yanagisawa M, Nakashima K, Takeda K, Ochiai W, Takizawa T, Ueno M, Takizawa M, Shibuya H, Taga T | title = Inhibition of BMP2-induced, TAK1 kinase-mediated neurite outgrowth by Smad6 and Smad7 | journal = Genes Cells | volume = 6 | issue = 12 | pages = 1091–9 | date = December 2001 | pmid = 11737269 | doi = 10.1046/j.1365-2443.2001.00483.x}} 16. ^{{cite journal | vauthors = Hanada M, Ninomiya-Tsuji J, Komaki K, Ohnishi M, Katsura K, Kanamaru R, Matsumoto K, Tamura S | title = Regulation of the TAK1 signaling pathway by protein phosphatase 2C | journal = J. Biol. Chem. | volume = 276 | issue = 8 | pages = 5753–9 | date = February 2001 | pmid = 11104763 | doi = 10.1074/jbc.M007773200 }} 17. ^{{cite journal | vauthors = Walsh MC, Kim GK, Maurizio PL, Molnar EE, Choi Y | title = TRAF6 autoubiquitination-independent activation of the NFkappaB and MAPK pathways in response to IL-1 and RANKL | journal = PLoS ONE | volume = 3 | issue = 12 | pages = e4064 | pmid = 19112497 | pmc = 2603309 | doi = 10.1371/journal.pone.0004064 | editor1-last = Unutmaz | editor1-first = Derya | year = 2008 }} 18. ^{{cite journal | vauthors = Sorrentino A, Thakur N, Grimsby S, Marcusson A, von Bulow V, Schuster N, Zhang S, Heldin CH, Landström M | title = The type I TGF-beta receptor engages TRAF6 to activate TAK1 in a receptor kinase-independent manner | journal = Nat. Cell Biol. | volume = 10 | issue = 10 | pages = 1199–207 | date = October 2008 | pmid = 18758450 | doi = 10.1038/ncb1780 }} Further reading{{refbegin |35em}}
1 : EC 2.7.11 |
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