IndraLab

Statements

OTUD5 binds TRIP12. 14 / 14
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"First, whether TRIP12 constitutively associates with OTUD5 is unknown."
40128189
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"TRIP12–OTUD5 antagonism regulates TNF-α–induced NF-κB signaling."
40128189
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"We next verified TRIP12–OTUD5 antagonism in TNF-α–induced NF-κB signaling."
40128189
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"The data presented thus far indicate that OTUD5 is cooperatively modified by K29-specific TRIP12 and K48-specific UBR5, resulting in the conjugation of K29/K48-linked branched ubiquitin chains, and the biological importance of TRIP12–OTUD5 antagonism is observed in TNF-α–induced NF-κB signaling."
40128189
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"Collectively, these results indicate that TRIP12 interacts with OTUD5 and promotes its ubiquitylation and degradation."
40128189
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"The biological importance of the TRIP12–OTUD5 interplay was demonstrated in the regulation of NF-κB signaling."
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"Because the simultaneous knockdown of OTUD5 partially restores NF-κB signaling under TRIP12 knockdown, the TRIP12–OTUD5 antagonism may account for the regulatory function of TRIP12 in NF-κB signaling."
40128189
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"This equilibrium favors ubiquitin chain assembly and subsequent OTUD5 degradation when TRIP12 interacts with OTUD5; UBR5 assembles K48-linked ubiquitin chains onto previously formed K29-linked chains more efficiently than de novo ubiquitylation (Fig.  xref ), presumably through ubiquitin interaction of the UBA domain (Fig.  xref and ref. xref )."
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"TRIP12 interacted with OTUD5 during co-immunoprecipitation (Fig.  xref )."
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"Whether the TRIP12–OTUD5 axis also regulates other pathways should be studied further."
40128189
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"TRIP12–OTUD5 antagonism regulates NF-κB signaling."
40128189
reach
"First, whether TRIP12 constitutively associates with OTUD5 is unknown."
40128189
reach
"Because UBR5 appears to stably associate with OTUD5 , and because TRIP12 possesses phosphorylation sites (https://www.phosphosite.org), we presume that TRIP12 may associate with OTUD5 under certain cellular conditions, triggering rapid OTUD5 degradation to fulfill cellular demand.Second, our model suggests complex ubiquitin architectures consisting of K29 and K48 linkages."
40128189
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"These results suggested that TRIP12–OTUD5 antagonism may regulate the NF-κB inflammatory signaling pathway."
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