IndraLab

Statements


2 | 2 8

reach
"Given that USP14 reversibly associates with PSMD2, we reasoned that TRIM11 might impede the USP14-PSMD2 interaction."

sparser
"USP14 binds to PSMD2, while UCHL5 can form a complex with PSMD4 and ADRM1 ( xref ; xref ; xref )."

reach
"Indeed, the association between endogenous USP14 and PSMD2 was strongly inhibited upon TRIM11 overexpression, as shown by reciprocal co-IP assays using anti-USP14 and anti-PSMD2 antibodies."

sparser
"USP14 binds to the Rpn1 subunit in the base of the 19S RP ( Stone et al., 2004; Leggett et al., 2002 ), however USP14 does not appear to be a constituent subunit and can be dissociated from the protea[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

sparser
"Given that USP14 reversibly associates with PSMD2 (refs. xref , xref ), we reasoned that TRIM11 might impede the USP14-PSMD2 interaction."

No evidence text available

sparser
"This mode of targeting could be ubiquitin-independent because the substrate is presented to the proteasome by its positioning near the Usp14-Rpn1 region through the action of the ligand, without the requirement of previous ubiquitination."

No evidence text available

sparser
"Among them, PSMD2 appeared to be the most abundant, consistent with the previous finding that USP14 binds to the proteasome via PSMD2 (ref. xref )."

sparser
"Consistently, silencing TRIM28 using two independent shRNAs (Supplementary Fig.  xref ) failed to alter the levels of insoluble K48 polyUb conjugates (Supplementary Fig.  xref ) or the USP14-PSMD2 interaction (Supplementary Fig.  xref ), underscoring the specific effect of TRIM11 on the proteasome."

sparser
"Together, these results show that TRIM11 inhibits the association of USP14 with PSMD2, preventing it from docking on the proteasome."

sparser
"USP14 reversibly associates with the Rpn1 subunit of the 19S RP base xref xref xref , and presumably dissociated from the proteasomes during centrifugation."