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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 *

• IRef Biogrid Interaction: TBK1 — RELA (direct interaction, enzymatic study) Fujita et al., Mol Cell Biol 2003*
• IRef Biogrid Interaction: TBK1 — RELA (physical association, affinity chromatography technology) Bouwmeester et al., Nat Cell Biol 2004
• IRef Biogrid Interaction: TBK1 — RELA (direct interaction, enzymatic study) Buss et al., J Biol Chem 2004*
• IRef Hprd Interaction: TBK1 — RELA (in vitro) Fujita et al., Mol Cell Biol 2003*

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