IndraLab

Statements


OTUB1 inhibits UBE2D2. 7 / 9
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"The OTUB1 double E28A D35A substitution, which affects OTUB1 contacts with UBCH5B, greatly decreased the ability of UBCH5B to stimulate OTUB1 DUB activity without affecting OTUB1 activity in the absence of UBCH5B (XREF_FIG)."

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"Similar interactions could form between OTUB1 and UBE2D2 (UBCH5b) (XREF_FIG), but clashes due to an insertion and a non conserved lysine would arise with UBE2L3 (UBCH7), consistent with the observation that OTUB1 inhibits UBCH5b but not UBCH7 4."

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"Interestingly, this non canonical mode of action by OTUB1 was found not to be unique to UBC13, as OTUB1 was also found to interact with and inhibit the E2 enzymes UBE2D2 and UBCH5B and UBE2D3 and UBCH[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"Competition with E3 binding is likely to be particularly important for OTUB1 inhibition of UBCH5b, which, unlike UBC13, is strictly dependent upon an E3 ligase for activity."

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"Since OTUB1 also inhibits UBCH5b 4, which does not function with a UEV, we speculate that the OTUB1 N-terminus may also interfere with acceptor ubiquitin binding for other E2s."

sparser
"Competition with E3 binding is likely to be particularly important for OTUB1 inhibition of UBCH5b, which, unlike UBC13, is strictly dependent upon an E3 ligase for activity."

sparser
"Similar interactions could form between OTUB1 and UBE2D2 (UBCH5b) ( xref ), but clashes due to an insertion and a non-conserved lysine would arise with UBE2L3 (UBCH7), consistent with the observation that OTUB1 inhibits UBCH5b but not UBCH7 xref ."