IndraLab

Statements

OTUD5 is ubiquitinated. 7 / 7
| 7
sparser
"UBR5 expression promoted both K29- and K48-linked ubiquitylation of OTUD5, which was almost completely diminished by TRIP12 knockdown (Fig.  xref , lanes 2, 4, 6, and 8)."
40128189
sparser
"However, the TRIP12-dependent K29-linked ubiquitylation of OTUD5 was partially decreased by UBR5 knockdown, whereas TRIP12-dependent increase of K48-linked chains was massively diminished by UBR5 knockdown (Fig.  xref , lanes 2, 4, 6, and 8)."
40128189
sparser
"TRIP12 promotes OTUD5 ubiquitylation and degradation."
40128189
sparser
"Next, we investigated whether OTUD5 DUB activity counteracted OTUD5 ubiquitylation by TRIP12 or UBR5."
40128189
sparser
"We also confirmed that TRIP12 knockdown decreased ubiquitylation of endogenous OTUD5 under proteasomal inhibition (Fig.  xref )."
40128189
sparser
"We subsequently investigated whether TRIP12 promoted ubiquitylation of OTUD5 in cell and in vitro."
40128189
sparser
"Using TUBE2 (tandem ubiquitin-binding entity 2), which serves as a pan-ubiquitin chain binder when four repeats of the UBA1 domains from HR23A are tandemly fused xref , we found that OTUD5 pan-ubiquitylation was enhanced by the expression of wild-type, but not catalytically inactive (C1959A), TRIP12 (Fig.  xref )."
40128189