IndraLab

Statements

OTUB1 binds DOA1. 9 / 9
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"Otu1 and Ufd3 only interact via the chaperone ( Figure 4 H), and, because the two cofactors use different docking sites on the chaperone, Cdc48 can bind Ufd3 and Otu1 at the same time, making a cooper[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Moreover, binding of Ufd3 and Otu1 to Spt23 p90 was strongly impaired in the ufd1-2 temperature-sensitive mutant ( Figure 5 D), suggesting that the substrate must first be recruited to the Cdc48 chape[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"The DUB Otu1 can bind simultaneously with Ufd3 to Cdc48."
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"Moreover, binding of Ufd3 and Otu1 to Spt23 p90 was strongly impaired in the ufd1-2 temperature-sensitive mutant ( Figure 5 D), suggesting that the substrate must first be recruited to the Cdc48 chape[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"In yeast, DUB-E3 complexes appear to play a similar role, as evidenced by the interaction of Ufd3 (a ubiquitin ligase) and Otu1 (a DUB) on Cdc48 complexes that regulate proteasomal degradation of substrates [ xref ]."
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"Rumpf and Jentsch [ xref ] outline a model by which the ubiquitylation and proteasome-targeting activity of VCP, when bound to the E4 ligase Ufd2, can be counteracted by either simultaneous binding of either the deubiquitylase Otu1 or the competing cofactor Ufd3."
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"An interesting implication of the genetic interaction between Ufd3 and Otu1 is that the two proteins may also be physically linked."
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"One view is that the binding of Otu1 and Ufd3 to the Cdc48 complex primes this enzyme to inhibit ubiquitination, and thus degradation, of ERAD substrates."
28159894
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"An interesting implication of the genetic interaction between Ufd3 and Otu1 is that the two proteins may also be physically linked."
16427015