IndraLab

Statements


USP15 is ubiquitinated. 6 / 6
| 6

sparser
"Both USP15 and Nef were ubiquitylated."

sparser
"Ubiquitylation of USP15 is clearly increased by co-expression of wild-type but not an E2 binding-deficient mutant of myc-BRAP ( xref B , compare lanes 5 with 4 and 12 with 11 )."

sparser
"Moreover, SYVN1 promotes T-cell immunity [ xref ], B-cell immunity [ xref ] and regulates TLR-induced inflammation through K27-linked ubiquitination and inactivation of Usp15 [ xref ]."

sparser
"Co-expression with neither the USP15 C298A mutant nor USP15 variant 2 affected CARD9 ubiquitination, indicating that the removal of ubiquitin is linked to the catalytic activity of USP15."

sparser
"Since Ub attachment to proteins followed by degradation of the proteins by UPS plays an integral role in regulation of the fate of proteins, we investigated the possibility of ubiquitylation of Nef and USP15."

sparser
"Mechanisms to control USP15 activity within cells are suggested by evidence that USP15 is alternatively spliced [ xref , xref ] and can be ubiquitylated or phosphorylated [ xref , xref , xref – xref ]."