IndraLab

Statements


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sparser
"Otu1 binds via its UBX-like domain to the N domain of Cdc48, an interaction that stimulates its deubiquitination activity ( xref ; xref )."

sparser
"This altered deubiquitination rate is not attributable to impaired assembly of the Otu1-Cdc48 complex, as Otu1 bound equivalently to wild-type Cdc48 and all Walker mutants ( xref )."

sparser
"Indeed, free Otu1 has much lower deubiquitination activity than Otu1 bound to the Cdc48 complex ( xref )."

sparser
"Intriguingly, Otu1 binds to Cdc48's N domain ( Figure 4 G)."

reach
"Otu1 binding to Cdc48 counteracts the association of Cdc48 with Ufd2, an " E4 " Ub ligase that extends polyUb chains on conjugates XREF_BIBR."

sparser
"Notably, binding of Otu1 to the N domain of Cdc48 does not block binding of substrate-recruiting cofactors (see above), indicating that the six N domains of the hexameric chaperone may bind different [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

sparser
"Otu1 binding to Cdc48 counteracts the association of Cdc48 with Ufd2, an “E4” Ub ligase that extends polyUb chains on conjugates xref ."

sparser
"Furthermore, the Cdc48-bound deubiquitinase Otu1 and the E4 ligase Ufd2 may edit and extend substrate-attached ubiquitin modifications at Cdc48 to promote binding to the proteasome and restrain competing rebinding to adaptors for Cdc48."

reach
"These data suggest that different members of the Cdc48 hexameric ring bind Otu1 versus Npl4 and Ufd1."

reach
"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."

reach
"We also show that Otu1 interacts with Cdc48, a regulator of the ER associated degradation pathway."

sparser
"Otu1 binding to the N-terminus of Cdc48 does not interfere with binding of the Cdc48 cofactors, Npl4 and Ufd1, which are vital to recognize ubiquitinated substrates [ xref , xref , xref ]."

sparser
"The DUB Otu1 interacts with Cdc48 to trim the polyubiquitin chain (but does not completely remove the chain) facilitating further threading of the substrate through the central pore of Cdc48."

reach
"The DUB Otu1 can bind simultaneously with Ufd3 to Cdc48."

reach
"This altered deubiquitination rate is not attributable to impaired assembly of the Otu1 and Cdc48 complex, as Otu1 bound equivalently to wild-type Cdc48 and all Walker mutants (XREF_SUPPLEMENTARY)."

sparser
"Our data indicate that the Otu1Cdc48 interaction is conserved among eukaryotes."

reach
"YOD1 is the closest homolog of Saccharomyces cerevisiae Otu1, which associates with Cdc48, to regulate the processing of the endoplasmic reticulum (ER) membrane embedded transcription factor Spt23 [18[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

reach
"YOD1 is the closest homolog of S. cerevisiae Otu1, which associates with Cdc48, to regulate the processing of the ER-membrane embedded transcription factor Spt23, a crucial component of the OLE pathway."

sparser
"We also show that Otu1 interacts with Cdc48, a regulator of the ER-associated degradation pathway."

sparser
"The DUB Otu1 binds to the N domains of Cdc48, and cleaves the ubiquitin chain following ATP hydrolysis by the D1 domains, which triggers the movement of the N domains to their “down-conformation”."

sparser
"Yeast two-hybrid assays confirmed a direct interaction of Otu1 with Cdc48 mediated via an N-terminally located UBX-like domain in Otu1."

sparser
"Interestingly, Otu1 and Ufd1/Npl4 can bind to the Cdc48 hexamer concomitantly and, unlike Ufd2, Otu1 can coexist with Ufd3 in the same complex [80] ."

sparser
"Thus, substrate release from Cdc48-UN depends on both Otu1 binding to Cdc48 ( xref ) and the deubiquitination activity of Otu1 ( xref )."

sparser
"In fact, we found also that Otu1 binds Cdc48 via this domain, as a GST-fusion protein that carries only the UBX-like domain of Otu1 bound Cdc48 equally as well as the full-length Otu1 protein (or a mu[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

sparser
"Importantly, Ubx5 did not bind to the Cdc48-UN-Otu1 complex unless polyubiquitinated substrate was added (lane 5 versus 4)."