Abstract
Ubiquitin (Ub) and ubiquitin-like proteins (UBLs) form an indispensable regulatory layer in human cell biology [1,2]. Cascades of approximately nine activating (E1) enzymes, ~40 conjugating (E2) enzymes, and >600 (E3) ligases can covalently attach distinct topologies of Ub and some UBLs to substrate proteins. More than 100 proteases – deubiquitylating enzymes (DUBs) and deUBLylases – dynamically reverse these modifications (A–C) [1–4]. Other UBLs function mainly as noncovalent modifiers (B, bottom). Dysregulation of Ub/UBL systems is linked to various human diseases (C) [1,3–10].
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