IndraLab
Statements
USP28 is phosphorylated. 4 / 4
|
4
rlimsp
"Based on these and other data, it has been proposed that DDR-induced phosphorylation of USP28 leads to its dissociation from the Fbw7 ubiquitin ligase complex, allowing unchecked Myc degradation, and its subsequent association with DDR components, such as 53BP1, claspin, Nbs1, and Chk2, to promote their stabilization (Popov et al., 2007a)."