IndraLab

Statements

USP13 binds BAG6. 13 / 13
4 | 4 5
sparser
"We agree with the reviewers that the physical interaction of USP13 with the Bag6 complex makes it hard to distinguish whether the effect of USP13 knockdown on Bag6-SGTA interaction is due to lack of deubiquitination by USP13 or its scaffolding function."
24424410
reach
"Since Bag6 can interact with both gp78 and USP13, we asked whether these proteins could form a multiprotein complex."
24424410
biogrid
No evidence text available
24424410
biogrid
No evidence text available
38043062
reach
"We next tested whether USP13 could physically interact with Bag6 and/or its cofactors."
24424410
reach
"Because depletion of gp78 did not affect the interaction of USP13 with Bag6 (XREF_FIG, lane 7 vs 5), USP13 might bind Bag6 directly."
24424410
biogrid
No evidence text available
24424410
reach
"Taken together, these results suggest a direct interaction between USP13 and Bag6 that is mediated by the Bag6 UBL domain."
24424410
biogrid
No evidence text available
24424410
sparser
"By contrast, the cytosolic chaperone Hsp90 was not co-precipitated ( xref ), demonstrating a specific interaction between USP13 and the Bag6 complex."
24424410
sparser
"The interaction of USP13 with the Bag6 complex and gp78 did not require its deubiquitinating activity ( xref )."
24424410
sparser
"Because depletion of gp78 did not affect the interaction of USP13 with Bag6 ( xref , lane 7 vs 5), USP13 might bind Bag6 directly."
24424410
sparser
"However, given that USP13 can also interact physically with Bag6, it is also possible that USP13 may serve an adaptor function to promote Bag6–SGTA interaction."
24424410