journal article Oct 01, 2012

Targeting of TAK1 in inflammatory disorders and cancer

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References
93
[1]
Yamaguchi "Identification of a member of the MAPKKK family as a potential mediator of TGF-β signal transduction" Science (1995) 10.1126/science.270.5244.2008
[2]
Shirakabe "TAK1 mediates the ceramide signaling to stress-activated protein kinase/c-Jun N-terminal kinase" J. Biol. Chem. (1997) 10.1074/jbc.272.13.8141
[3]
Sakurai "TGF-β-activated kinase 1 stimulates NF-κB activation by an NF-κB-inducing kinase-independent mechanism" Biochem. Biophys. Res. Commun. (1998) 10.1006/bbrc.1998.8124
[4]
Ninomiya-Tsuji "The kinase TAK1 can activate the NIK-IκB as well as the MAP kinase cascade in the IL-1 signalling pathway" Nature (1999) 10.1038/18465
[5]
Sakurai "Functional interactions of transforming growth factor β-activated kinase 1 with IκB kinases to stimulate NF-κB activation" J. Biol. Chem. (1999) 10.1074/jbc.274.15.10641
[6]
Sorrentino "The type I TGF-β receptor engages TRAF6 to activate TAK1 in a receptor kinase-independent manner" Nat. Cell Biol. (2008) 10.1038/ncb1780
[7]
Yamashita "TRAF6 mediates Smad-independent activation of JNK and p38 by TGF-β" Mol. Cell (2008) 10.1016/j.molcel.2008.09.002
[8]
Landström "The TAK1–TRAF6 signalling pathway" Int. J. Biochem. Cell Biol. (2010) 10.1016/j.biocel.2009.12.023
[9]
Yamazaki "Two mechanistically and temporally distinct NF-κB activation pathways in IL-1 signaling" Sci. Signal. (2009) 10.1126/scisignal.2000387
[10]
Shibuya "TAB1: an activator of the TAK1 MAPKKK in TGF-β signal transduction" Science (1996) 10.1126/science.272.5265.1179
[11]
Takaesu "TAB2, a novel adaptor protein, mediates activation of TAK1 MAPKKK by linking TAK1 to TRAF6 in the IL-1 signal transduction pathway" Mol. Cell (2000) 10.1016/s1097-2765(00)80244-0
[12]
Ishitani "Role of the TAB2-related protein TAB3 in IL-1 and TNF signaling" EMBO J. (2003) 10.1093/emboj/cdg605
[13]
Sato "Essential function for the kinase TAK1 in innate and adaptive immune responses" Nat. Immunol. (2005) 10.1038/ni1255
[14]
Shim "TAK1, but not TAB1 or TAB2, plays an essential role in multiple signaling pathways in vivo" Genes Dev. (2005) 10.1101/gad.1360605
[15]
Sekimoto "Targeted disruption of the Tab1 gene causes embryonic lethality and defects in cardiovascular and lung morphogenesis" Mech. Dev. (2002) 10.1016/s0925-4773(02)00391-x
[16]
Sanjo "TAB2 is essential for prevention of apoptosis in fetal liver but not for interleukin-1 signaling" Mol. Cell. Biol. (2003) 10.1128/mcb.23.4.1231-1238.2003
[17]
Singhirunnusorn "Critical roles of threonine 187 phosphorylation in cellular stress-induced rapid and transient activation of transforming growth factor-β-activated kinase 1 (TAK1) in a signaling complex containing TAK1-binding protein TAB1 and TAB2" J. Biol. Chem. (2005) 10.1074/jbc.m407537200
[19]
Pathak "O-GlcNAcylation of TAB1 modulates TAK1-mediated cytokine release" EMBO J. (2000) 10.1038/emboj.2012.8
[20]
Chen "Ubiquitination in signaling to and activation of IKK" Immunol. Rev. (2012) 10.1111/j.1600-065x.2012.01108.x
[21]
Tokunaga "LUBAC, a novel ubiquitin ligase for linear ubiquitination, is crucial for inflammation and immune responses" Microbes Infect. (2012) 10.1016/j.micinf.2012.01.011
[22]
Kulathu "Two-sided ubiquitin binding explains specificity of the TAB2 NZF domain" Nat. Struct. Mol. Biol. (2009) 10.1038/nsmb.1731
[23]
Komander "Molecular discrimination of structurally equivalent Lys 63-linked and linear polyubiquitin chains" EMBO Rep. (2009) 10.1038/embor.2009.55
[24]
Sato "Structural basis for specific recognition of Lys 63-linked polyubiquitin chains by NZF domains of TAB2 and TAB3" EMBO J. (2009) 10.1038/emboj.2009.345
[25]
Fan "Lysine 63-linked polyubiquitination of TAK1 at lysine 158 is required for tumor necrosis factor α- and interleukin-1β-induced IKK/NF-κB and JNK/AP-1 activation" J. Biol. Chem. (2010) 10.1074/jbc.m109.076976
[26]
Xia "Direct activation of protein kinases by unanchored polyubiquitin chains" Nature (2009) 10.1038/nature08247
[27]
Kajino "Protein phosphatase 6 down-regulates TAK1 kinase activation in the IL-1 signaling pathway" J. Biol. Chem. (2006) 10.1074/jbc.m608155200
[28]
Cheung "Feedback control of the protein kinase TAK1 by SAPK2a/p38α" EMBO J. (2003) 10.1093/emboj/cdg552
[29]
Ahmed "The E3 ligase Itch and deubiquitinase Cyld act together to regulate Tak1 and inflammation" Nat. Immunol. (2011) 10.1038/ni.2157
[30]
Fan "Lys(48)-linked TAK1 polyubiquitination at lysine-72 downregulates TNFα-induced NF-κB activation via mediating TAK1 degradation" Cell. Signal. (2012) 10.1016/j.cellsig.2012.02.017
[31]
Miyamoto "Nuclear initiated NF-κB signaling: NEMO and ATM take center stage" Cell Res. (2011) 10.1038/cr.2010.179
[32]
Hinz "A cytoplasmic ATM–TRAF6–cIAP1 module links nuclear DNA damage signaling to ubiquitin-mediated NF-κB activation" Mol. Cell (2010) 10.1016/j.molcel.2010.09.008
[33]
Wu "ATM- and NEMO-dependent ELKS ubiquitination coordinates TAK1-mediated IKK activation in response to genotoxic stress" Mol. Cell (2010) 10.1016/j.molcel.2010.09.010
[34]
TGFβ signalling: a complex web in cancer progression

Hiroaki Ikushima, Kohei Miyazono

Nature Reviews Cancer 2010 10.1038/nrc2853
[35]
Mao "TAK1 lysine 158 is required for TGF-β-induced TRAF6-mediated Smad-independent IKK/NF-κB and JNK/AP-1 activation" Cell. Signal. (2011) 10.1016/j.cellsig.2010.09.006
[36]
Kim "Transforming growth factor-β (TGF-β1) activates TAK1 via TAB1-mediated autophosphorylation, independent of TGF-β receptor kinase activity in mesangial cells" J. Biol. Chem. (2009) 10.1074/jbc.m109.007146
[37]
Várady "TTRAP is a novel component of the non-canonical TRAF6–TAK1 TGF-β signaling pathway" PLoS ONE (2011) 10.1371/journal.pone.0025548
[38]
Karin "NF-κB: linking inflammation and immunity to cancer development and progression" Nat. Rev. Immunol. (2005) 10.1038/nri1703
[39]
Wagner "Fos/AP-1 proteins in bone and the immune system" Immunol. Rev. (2005) 10.1111/j.0105-2896.2005.00332.x
[40]
Gaestel "Protein kinases as small molecule inhibitor targets in inflammation" Curr. Med. Chem. (2007) 10.2174/092986707781696636
[41]
Thome "Antigen receptor signaling to NF-κB via CARMA1, BCL10, and MALT1" Cold Spring Harb. Perspect. Biol. (2010) 10.1101/cshperspect.a003004
[42]
Sun "The TRAF6 ubiquitin ligase and TAK1 kinase mediate IKK activation by BCL10 and MALT1 in T lymphocytes" Mol. Cell (2004) 10.1016/s1097-2765(04)00236-9
[43]
Shinohara "PKCβ regulates BCR-mediated IKK activation by facilitating the interaction between TAK1 and CARMA1" J. Exp. Med. (2005) 10.1084/jem.20051591
[44]
Schuman "A critical role of TAK1 in B-cell receptor-mediated nuclear factor κB activation" Blood (2009) 10.1182/blood-2008-08-176057
[45]
Shinohara "IκB kinase β-induced phosphorylation of CARMA1 contributes to CARMA1 Bcl10 MALT1 complex formation in B cells" J. Exp. Med. (2007) 10.1084/jem.20070379
[46]
He "The transmembrane activator TACI triggers immunoglobulin class switching by activating B cells through the adaptor MyD88" Nat. Immunol. (2010) 10.1038/ni.1914
[47]
Wan "The kinase TAK1 integrates antigen and cytokine receptor signaling for T cell development, survival and function" Nat. Immunol. (2006) 10.1038/ni1355
[48]
Liu "Essential role of TAK1 in thymocyte development and activation" Proc. Natl. Acad. Sci. U.S.A. (2006) 10.1073/pnas.0603089103
[49]
Sato "TAK1 is indispensable for development of T cells and prevention of colitis by the generation of regulatory T cells" Int. Immunol. (2006) 10.1093/intimm/dxl082
[50]
Zhao "The deubiquitinase CYLD targets Smad7 protein to regulate transforming growth factor β (TGF-β) signaling and the development of regulatory T cells" J. Biol. Chem. (2011) 10.1074/jbc.m111.292961

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Cited By
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Nature Immunology
Mitogen-activated protein kinases in innate immunity

J. Simon C. Arthur, Steven C. Ley · 2013

Nature Reviews Immunology
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Citations
93
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Published
Oct 01, 2012
Vol/Issue
33(10)
Pages
522-530
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Cite This Article
Hiroaki Sakurai (2012). Targeting of TAK1 in inflammatory disorders and cancer. Trends in Pharmacological Sciences, 33(10), 522-530. https://doi.org/10.1016/j.tips.2012.06.007
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