IndraLab

Statements


USP8 is phosphorylated on tyrosine. 5 / 5
| 5

rlimsp
"Of note, serum starvation decreased the Tyr-phosphorylation levels of USP8 (Fig. 6a; lower panels) and FLAG-USP8 proteins (Fig. 6b; lower panels)."

rlimsp
"Consistent with the in vitro assays, EGFR knockdown significantly reduced the Tyr-phosphorylation levels of USP8 in serum-fed RPE1 cells (Fig. 8a)."

rlimsp
"To fully understand the underlying mechanism of USP8 activation, we searched for a Tyr kinase that is responsible for the phosphorylation of USP8."

rlimsp
"Since decreased USP8 tyrosine phosphorylation is associated with enhanced endosomal recycling of EGFR when cells are stimulated by TGFα, it is likely that USP8 phosphorylation may regulate its DUB activity."

rlimsp
"These data suggest that USP8 phosphorylation, possibly on Tyr residue(s), enhances its DUB activity."