IndraLab

Statements


USP15 is ubiquitinated. 12 / 12
| 12

sparser
"Moreover, we value the insightful suggestion regarding delving into the ubiquitination of USP15 through immunoprecipitation to elucidate changes in the RelA ubiquitination [50] ."

sparser
"Subsequent Western blot experiments revealed that PLOD2 upregulation diminished USP15 ubiquitination while augmenting Akt and mTOR phosphorylation [ xref ], suggesting that the PLOD2/USP15 axis modulates PI3K/Akt/mTOR pathway activation."

sparser
"The precise mechanism by which PLOD2 influences USP15 ubiquitination remains unclear, but it is conceivable that PLOD2 modifies USP15, reducing its activity and leading to increased ubiquitination and degradation of a negative regulator of the PI3K/Akt/mTOR pathway."

sparser
"Further studies are needed to identify the specific E3 ligase responsible for USP15 ubiquitination and the nature of the modification induced by PLOD2."

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
"Both USP15 and Nef were ubiquitylated."

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 ]."

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
"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
"The results demonstrated that in CRC cells, USP15 ubiquitination levels rose when PLOD2 expression was downregulated and decreased when PLOD2 was overexpressed (Figure  xref )."

sparser
"All the outcomes above suggested that PLOD2 increased USP15 expression by preventing the ubiquitination of USP15 protein for degradation in CRC cells."

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."