Ontology highlight
ABSTRACT:
SUBMITTER: Scott DC
PROVIDER: S-EPMC5091668 | biostudies-literature | 2016 Aug
REPOSITORIES: biostudies-literature
Scott Daniel C DC Rhee David Y DY Duda David M DM Kelsall Ian R IR Olszewski Jennifer L JL Paulo Joao A JA de Jong Annemieke A Ovaa Huib H Alpi Arno F AF Harper J Wade JW Schulman Brenda A BA
Cell 20160801 5
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 thioester-forming RBR-type E3, ARIH1, and rely on ARIH1 to directly add the first UB a ...[more]