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RELA — TAB1

Text-mined interactions from Literome

Ninomiya-Tsuji et al., Nature 1999 : Stimulation of TAK1 causes activation of NF-kappaB , which is blocked by dominant negative mutants of NIK, and an inactive TAK1 mutant prevents activation of NF-kappaB that is mediated by IL-1 but not by NIK
Irie et al., FEBS Lett 2000 : A kinase negative mutant of TAK1 inhibited the LPS induced NF-kappaB activation both in a macrophage-like cell line, RAW 264.7, and in human embryonic kidney 293 cells expressing toll-like receptor 2 or 4
Mizukami et al., Mol Cell Biol 2002 (MAP Kinase Signaling System) : Dominant negative forms of TAK1 and TAB2 inhibit NF-kappaB activation induced by overexpression of RANK ... Furthermore, in murine monocyte RAW 264.7 cells, dominant negative forms of TAK1 and TAB2 inhibit NF-kappaB activation induced by RANKL and endogenous TAK1 is activated in response to RANKL stimulation
Jiang et al., J Biol Chem 2003 (MAP Kinase Signaling System) : Kinase inactive mutants of TAK1 ( TAK1DN ) and PKR ( PKRDN ) inhibit poly ( dI.dC ) -induced TLR3 mediated NFkappaB activation, suggesting that both of these kinases play important roles in this pathway
Rannou et al., Joint Bone Spine 2006 (Arthritis, Rheumatoid) : When these cytokines bind to their membrane receptor, they set off signaling cascades, with activation of TGFbeta activating kinase ( TAK-1 ), of NF-kappaB by Ikappa-B kinase, of mitogen activated protein kinases ( MAP kinases ), and finally of activator protein-1 (AP-1)
Morlon et al., Hum Mol Genet 2005 (Ectodermal Dysplasia) : TAB2, TRAF6 and TAK1 are involved in NF-kappaB activation induced by the TNF-receptor, Edar and its adaptator Edaradd ... Moreover, we show that dominant negative forms of TAB2, TRAF6 and TAK1 blocked the NF-kappaB activation induced by Edaradd
Huang et al., Cell Death Differ 2006 : Osteoclast differentiation requires TAK1 and MKK6 for NFATc1 induction and NF-kappaB transactivation by RANKL ... TAK1-DN , MKK6-DN, and SB203580, but not MKK3-DN, also suppressed RANKL stimulation of NF-kappaB transcription activity in a manner dependent on p65 phosphorylation on Ser-536
Sethi et al., J Biol Chem 2006 : NF-kappaB reporter activity induced by TNFR1, TNF receptor associated death domain, TRAF2, TAK1 , NF-kappaB inducing kinase, and IKKbeta was inhibited by indirubin but not that induced by p65 transfection
Wan et al., Nat Immunol 2006 : In mature thymocytes, TAK1 was required for interleukin 7-mediated survival and T cell receptor dependent activation of transcription factor NF-kappaB and the kinase Jnk
Huangfu et al., J Biol Chem 2006 : We found that TAO2 ( thousand-and-one amino acid kinase 2 ) associates with TAK1 and can inhibit TAK1 mediated activation of NF-kappaB but not of JNK
Sethi et al., Blood 2007 (Neoplasm Invasiveness...) : Celastrol, a novel triterpene, potentiates TNF induced apoptosis and suppresses invasion of tumor cells by inhibiting NF-kappaB regulated gene products and TAK1 mediated NF-kappaB activation ... Recent studies indicate that TNF induced IKK activation requires activation of TAK1, and we indeed found that celastrol inhibited the TAK1 induced NF-kappaB activation
Pandey et al., J Biol Chem 2007 : As examined by DNA binding, we found that butein suppressed tumor necrosis factor (TNF) induced NF-kappaB activation in a dose- and time dependent manner ; suppressed the NF-kappaB activation induced by various inflammatory agents and carcinogens ; and inhibited the NF-kappaB reporter activity induced by TNFR1, TRADD, TRAF2, NIK, TAK1/TAB1 , and IKK-beta ... As examined by DNA binding, we found that butein suppressed tumor necrosis factor (TNF) induced NF-kappaB activation in a dose- and time dependent manner ; suppressed the NF-kappaB activation induced by various inflammatory agents and carcinogens ; and inhibited the NF-kappaB reporter activity induced by TNFR1, TRADD, TRAF2, NIK, TAK1/TAB1 , and IKK-beta
Suzuki et al., J Biol Chem 2007 (Cell Transformation, Viral...) : Constitutive activation of TAK1 by HTLV-1 tax dependent overexpression of TAB2 induces activation of JNK-ATF2 but not IKK-NF-kappaB
Pandey et al., Blood 2007 (Neoplasm Metastasis) : GA suppressed NF-kappaB activation induced by various inflammatory agents and carcinogens and this, accompanied by the inhibition of TAK1/TAB1 mediated IKK activation, inhibited IkappaBalpha phosphorylation and degradation, suppressed p65 phosphorylation and nuclear translocation, and finally abrogated NF-kappaB dependent reporter gene expression
Yang et al., J Biol Chem 2007 (Tuberculosis) : We also demonstrate a requirement for the E2-conjugating enzyme Ubc13, the E3 ubiquitin ligase Traf6, and the ubiquitin activated kinase Tak1 in Nod2 mediated NF-kappaB activation
Neil et al., Cancer Res 2008 (Disease Progression) : Expression of a truncated TAB1 mutant [ i.e., TAB1 ( 411 ) ] reduced basal and TGF-beta mediated NF-kappaB activation in NMuMG cells driven to undergo EMT by TGF-beta and in 4T1 cells stimulated by TGF-beta
Sethi et al., Mol Cancer Ther 2008 (Neoplasm Invasiveness...) : Pinitol also suppressed the NF-kappaB reporter activity induced by tumor necrosis factor receptor (TNFR)-1, TNFR associated death domain, TNFR associated factor-2, transforming growth factor-beta activated kinase-1 ( TAK-1 ) /TAK1 binding protein-1 , and IkappaBalpha kinase but not that induced by p65
Tang et al., J Exp Med 2008 (Bone Marrow Diseases...) : Activation of TAK1 by proinflammatory cytokines and T and B cell receptors induces the nuclear localization of nuclear factor kappaB (NF-kappaB) and the activation of c-Jun N-terminal kinase (JNK)/AP1 and P38, which play important roles in mediating inflammation, immune responses, T and B cell activation, and epithelial cell survival
Yu et al., J Biol Chem 2008 : Consistently, TAK1 mutant with alanine substitution of these two residues severely inhibits IL-1 induced NFkappaB and AP-1 activities, whereas TAK1 mutant with replacement of these two sites with acidic residues slightly enhances IL-1 induced NFkappaB and AP-1 activities compared with the TAK1 wild-type
Zhou et al., World J Gastroenterol 2008 (Adenocarcinoma...) : Viable LBG or LBG- ( s ) pretreatment attenuated the expression of TLR4, inhibited the phosphorylation of TAK1 and p38MAPK, prevented the activation of NF-kappaB , and consequently blocked IL-8 production
Fraczek et al., J Biol Chem 2008 : The kinase activity of IL-1 receptor associated kinase 4 is required for interleukin-1 receptor/toll-like receptor induced TAK1 dependent NFkappaB activation
Schuman et al., Blood 2009 : The kinase TAK1 is essential for T-cell receptor ( TCR ) -mediated nuclear factor kappaB (NF-kappaB) activation and T-cell development ... However, the role of TAK1 in B-cell receptor (BCR) mediated NF-kappaB activation and B-cell development is not clear ... Thus, TAK1 is critical for B-cell maturation and BCR induced NF-kappaB activation
Yamaguchi et al., Cell Biol Int 2009 (MAP Kinase Signaling System) : JNK binding protein 1 regulates NF-kappaB activation through TRAF2 and TAK1
Henmi et al., Biochem J 2009 : TAK1 ( transforming-growth-factor-beta activated kinase 1 ) mediates the IL-1 signalling pathway to NF-kappaB, and we observed that the TAK1 induced activation of NF-kappaB was suppressed by PP2Ceta-2 expression
Lee et al., Biochim Biophys Acta 2009 : DSCR1-1S also stimulated IL-1R mediated signaling pathways, TAK1 activation, NF-kappaB transactivation , and IL-8 production, all downstream consequences of IL-1R activation
Yamazaki et al., Science signaling 2009 : Here, we showed that TAK1 mediated activation of NF-kappaB required the transient formation of a signaling complex that included tumor necrosis factor receptor associated factor 6 ( TRAF6 ), MEKK3, and TAK1
Cheng et al., J Biomed Mater Res A 2010 (Inflammation...) : The critical role for TAK1 in p38MAPK and NFkappaB activation was as well confirmed by the inhibition of p38MAPK and NFkappaB activity following 5Z-7-oxozeaenol, a selective inhibitor of TAK1
Lluis et al., PloS one 2010 : Overexpression of IKK2-EE, a constitutive activator of NF-kappaB, protected TAK1-/- MEFs against TRAIL killing, suggesting that TAK1 activation of NF-kappaB is critical for the viability of cells treated with TRAIL
Srivastava et al., J Biol Chem 2010 : Although both the TAK1 and the CARMA1 binding sites in ADAP are essential for IkappaB alpha phosphorylation and degradation and NF-kappaB nuclear translocation, only the TAK1 binding site in ADAP is necessary for IKK phosphorylation