NEDD8 and ubiquitin ligation by cullin-RING E3 ligases.
Journal
Current opinion in structural biology
ISSN: 1879-033X
Titre abrégé: Curr Opin Struct Biol
Pays: England
ID NLM: 9107784
Informations de publication
Date de publication:
04 2021
04 2021
Historique:
received:
15
09
2020
revised:
04
10
2020
accepted:
05
10
2020
pubmed:
8
11
2020
medline:
16
10
2021
entrez:
7
11
2020
Statut:
ppublish
Résumé
RING E3s comprise the largest family of ubiquitin (UB) and ubiquitin-like protein (UBL) ligases. RING E3s typically promote UB or UBL transfer from the active site of an associated E2 enzyme to a distally-recruited substrate. Many RING E3s - including the cullin-RING ligase family - are multifunctional, interacting with various E2s (or other E3s) to target distinct proteins, transfer different UBLs, or to initially modify substrates with UB or subsequently elongate UB chains. Here we consider recent structures of cullin-RING ligases, and their partner E2 enzymes, representing ligation reactions. The studies collectively reveal multimodal mechanisms - interactions between ancillary E2 or E3 domains, post-translational modifications, or auxiliary binding partners - directing cullin-RING E3-E2 enzyme active sites to modify their specific targets.
Identifiants
pubmed: 33160249
pii: S0959-440X(20)30174-3
doi: 10.1016/j.sbi.2020.10.007
pmc: PMC8096640
mid: NIHMS1644264
pii:
doi:
Substances chimiques
Cullin Proteins
0
Ubiquitin
0
Ubiquitins
0
Ubiquitin-Protein Ligases
EC 2.3.2.27
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
101-109Subventions
Organisme : NCI NIH HHS
ID : P30 CA021765
Pays : United States
Organisme : NCI NIH HHS
ID : R01 CA247365
Pays : United States
Informations de copyright
Copyright © 2020 The Authors. Published by Elsevier Ltd.. All rights reserved.
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