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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