1941 Twists and turns in ubiquitin-like protein conjugation cascades
Brenda A. Schulman
Post-translational modification by ubiquitin-like proteins (UBLs) is a primary eukaryotic means of protein regulation. This highly dynamic, multistep, multienzyme process involves sequential transport of an entire protein—the UBL—between multiple enzyme active sites within an E1 enzyme, then, transiently onto an E2 enzyme, and ultimately with assistance of an E3 enzyme onto a target protein. The structures and interactions of E1, E2, and E3 enzymes are themselves dynamic, and plasticity of enzyme conformations—from wholesale domain rotations to complete remodeling of portions of structures—helps mediate UBL ligation to targets in a specific manner. This review highlights some recent glimpses into enzyme dynamics in UBL modification pathways.