Structural insights into the activation of USP46 by WDR48 and WDR20

摘要

Ubiquitination is an important and reversible posttranslationalmodification that regulates the stability, localization,and function of proteins in many cellular processes.Deubiquitinases (DUBs) are responsible for the removal ofubiquitin chains from proteins, and ubiquitin-specificproteases (USPs) are the largest family of DUBs whichshare a conserved USP catalytic domain1. The USP domainconsists of three subdomains named as fingers, palm, andthumb. The catalytic center comprised of a conserved triad(Cys, Asp, and His) is located at the interface of the palm andthumb subdomains, and the fingers subdomain is involved inthe binding of Ub. The activity of USPs can be regulatedthrough various ways including, posttranslational modification,allosteric regulation, and interaction of binding partner2.