Yogesh Kulathu

Abstract The ubiquitin-specific proteases (USPs) family is the largest family of human deubiquitinating enzymes (DUBs). While most USPs are agnostic to polyubiquitin linkage-type, their substrate specificity is thought to be mediated by the recognition of the ubiquitnated protein itself. In addition to their catalytic domain, USPs have one or more auxiliary domains (ADs) with key functions in regulating DUB activity and localization.

Keywords selective autophagy selective autophagy receptor proteostasis ATG8 aggrephagy protein aggregate heat stress autophagic flux receptor evolution proteotoxic stress Introduction Macroautophagy (hereafter autophagy) is essential for maintaining organismal homeostasis amid fluctuating environmental conditions.1 It recycles damaged or unnecessary macromolecules and organelles, facilitating cellular renewal and adaptation.2 Autophagy enables organisms to withstand a wide spectrum of abiotic...

Abstract Reversible modification of target proteins by ubiquitin and ubiquitin-like proteins (UBLs) is widely used by eukaryotic cells to control protein fate and cell behaviour1. UFM1 is a UBL that predominantly modifies a single lysine residue on a single ribosomal protein, uL24 (also called RPL26), on ribosomes at the cytoplasmic surface of the endoplasmic reticulum (ER)2,3.