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RELA — TBK1
Protein-Protein interactions - manually collected from original source literature:
Studies that report less than 10 interactions are marked with *
Text-mined interactions from Literome
Pomerantz et al., EMBO J 1999
:
Kinase-inactive
TBK1 inhibits TANK mediated
NF-kappaB activation but does not block the activation mediated by TNF-alpha, IL-1 or CD40
Bonnard et al., EMBO J 2000
:
However,
T2K has a unique role in the activation of NF-kappaB directed transcription, apparently
independent of I-kappaB degradation and
NF-kappaB DNA binding
Wang et al., FEBS Lett 2004
:
A20 also inhibited TRIF-, but not its downstream signaling components
TBK1- , IKKbeta-, and IKKepsilon mediated
activation of ISRE and
NF-kappaB and IFN-beta promoter
Youn et al., J Immunol 2005
:
Furthermore, resveratrol inhibited the kinase activity of
TANK binding kinase 1 and the
NF-kappaB activation induced by RIP1 in RAW264.7 cells
Song et al., Proc Natl Acad Sci U S A 2008
:
Association with active LMP1 signaling complexes was also critical for IRF7 activation because (i) a dominant negative IRF7 bound to LMP1, blocked IRF7 association and activation, but did not
inhibit LMP1 induced
NF-kappaB or
TBK1 or Sendai virus mediated IFN stimulated response element activation ; and ( ii ) two different LMP1 transmembrane domain mutants, which fail to aggregate, each bound IRF7 and prevented LMP1 from binding and activating IRF7 in the same cell, but did not prevent NF-kappaB activation
Lee et al., Biochem Pharmacol 2009
:
Luteolin attenuated ligand independent activation of IRF3 or
NFkappaB induced by TLR4, TRIF, or
TBK1 , while it did not inhibit TLR oligomerization
Barbie et al., Nature 2009
(Lung Neoplasms...) :
In these cells,
TBK1 activated
NF-kappaB anti-apoptotic signals involving c-Rel and BCL-XL ( also known as BCL2L1 ) that were essential for survival, providing mechanistic insights into this synthetic lethal interaction
Delhase et al., Proc Natl Acad Sci U S A 2012
:
TBK1 induced
RelA phosphorylation results in inducible expression of plasminogen activator inhibitor-2 ( PAI-2 ), a member of the serpin family with known antiapoptotic activity