IndraLab

Statements


3 | 4 11

sparser
"It appears that the second UBA domain is crucial for USP13 to bind gp78."

sparser
"The requirement of gp78 interaction for ERAD inhibition by ectopic USP13 indicates that the interaction of USP13 with gp78 is functionally relevant to ERAD."

No evidence text available

No evidence text available

No evidence text available

sparser
"Importantly, USP13 associates with AMFR to prevent polyubiquitylation of UBL4A, protecting the BAG6 complex from proteasomal degradation and maintaining proper ERAD pathway function [ xref ]."

sparser
"Thus, the association of USP13 with AMFR prevents collateral damage in the ERAD pathway by promoting the distinction between bona fide ERAD substrates and protein complexes that ERAD pathway E3s must engage to ensure proper substrate shuttling for degradation."

sparser
"Interestingly, USP13 associates with gp78 to attenuate polyubiquitination of ubiquitin-like protein 4A (UBL4A), a part of the Bag6 complex that helps chaperone retrotranslocated ERAD substrates to the proteasome, thereby protecting the Bag6 complex from proteasomal degradation and maintaining an adequate ERAD pathway, highlighting the importance of the associated DUB activity during ERAD [ xref ]."

sparser
"Recently, cleaved Bag6 induced by caspase three activation was reported to interact with LC3-Ⅰ and pro-LC3 under ER stress conditions such as gp78 overexpression and USP13 downregulation, leading to autophagy inhibition and apoptosis activation ( xref )."

reach
"USP13 interacts directly with gp78 in ERAD."

reach
"Several lines of evidence confirmed that gp78 could bind to USP13 directly and promote its interaction with p97."

sparser
"Our study reveals an unexpected interaction between USP13 and the ERAD-specific ubiquitin ligase gp78."

reach
"An endogenous interaction between USP13 and gp78 was also detected (XREF_FIG)."

reach
"These results demonstrated a specific and direct interaction between USP13 and gp78 that facilitates USP13-p97 association."

sparser
"This result is consistent with our model that ERAD inhibition by USP13 overexpression is probably achieved by blocking functional protein–protein interactions required for ERAD through the binding of USP13 with gp78."

sparser
"USP13 interacts directly with gp78 in ERAD."

sparser
"Several lines of evidence confirmed that gp78 could bind to USP13 directly and promote its interaction with p97."

sparser
"An endogenous interaction between USP13 and gp78 was also detected ( xref )."