Article
Two Distinct Types of E3 Ligases Work in Unison to Regulate Substrate Ubiquitylation.
Cell - 25 Aug 2016
Scott Daniel C, Rhee David Y, Duda David M, Kelsall Ian R, Olszewski Jennifer L, Paulo Joao A, de Jong Annemieke, Ovaa Huib, Alpi Arno F, Harper J Wade, Schulman Brenda A
Abstract excerpt
Hundreds of human cullin-RING E3 ligases (CRLs) modify thousands of proteins with ubiquitin (UB) to achieve vast regulation. Current dogma posits that CRLs first catalyze UB transfer from an E2 to their client substrates and subsequent polyubiquitylation from various linkage-specific E2s. We report an alternative E3-E3 tagging cascade: many cellular NEDD8-modified CRLs associate with a mechanistically distinct...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.