IndraLab

Statements

TRAF3 binds OTUD7B. 8 / 8
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"In response to noncanonical NF-kappaB stimuli, Otud7b binds and deubiquitinates TRAF3, thereby inhibiting TRAF3 proteolysis and preventing aberrant noncanonical NF-kappaB activation."
23334419
reach
"Non-canonical NF-κB activators induce the interaction of OTUD7B and TRAF3, thereby down-regulating TRAF3 ubiquitination and degradation and preventing aberrant non-canonical NF-κB activation."
32958760
sparser
"Notably, OTUD7B directly binds to TRAF3 rather than to NIK and deubiquitinates TRAF3, thereby inhibiting TRAF3 proteolysis and preventing NIK accumulation and NF-κB pathway activation."
33198776
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"We found that Traf3 physically interacted with Otud7b in T cells (unpublished data), although we could not detect appreciable degradation of Traf3 along with TCR-CD28 ligation in either WT or Otud7b deficient T cells."
26903241
sparser
"Non-canonical NF-κB activators induce the interaction of OTUD7B and TRAF3, thereby down-regulating TRAF3 ubiquitination and degradation and preventing aberrant non-canonical NF-κB activation."
32958760
sparser
"We found that Traf3 physically interacted with Otud7b in T cells (unpublished data), although we could not detect appreciable degradation of Traf3 along with TCR–CD28 ligation in either WT or Otud7b-deficient T cells."
26903241
reach
"Upon ligation of these receptors, Otud7b binds to TRAF3, and this inducible interaction requires a ubiquitin association (UBA) domain present in the N-terminus of Otud7b, suggesting the possibility that ubiquitination of TRAF3 may facilitate its binding by Otud7b."
26085207
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"Activation of BAFFR increases OTUD7B expression and the newly synthesized deubiquitinase then binds to TRAF3 resulting in the formation of a high molecular weight complex including OTUDB7, TRAF3, TRAF2, and cIAP1/2."
30349534