IndraLab
Statements
"USP20 is regulated by HERC2 following DNA damage or replication stress.The HECT domain of WT HERC but not the catalytic inactive mutant (CA) ubiquitinated USP20 in vitro (Figure (Figure4G).4G). Taken together, these results suggested that HERC2 functions as an E3 ligase of USP20 and negatively regulates USP20 in unstressed cells."
"HERC2 promotes USP20 degradation.|Under unperturbed condition, HERC2 ubiquitinates USP20 and promotes ubiquitination mediated proteasomal degradation of USP20, regulating the status of K48 linked polyubiquitination of CLASPIN and ensuring appropriate protein levels of CLASPIN during the S-phase."