A conserved N-terminal motif of CUL3 contributes to assembly and E3 ligase activity of CRL3
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
06 May 2024
06 May 2024
Historique:
received:
12
10
2023
accepted:
19
04
2024
medline:
7
5
2024
pubmed:
7
5
2024
entrez:
6
5
2024
Statut:
epublish
Résumé
The CUL3-RING E3 ubiquitin ligases (CRL3s) play an essential role in response to extracellular nutrition and stress stimuli. The ubiquitin ligase function of CRL3s is activated through dimerization. However, how and why such a dimeric assembly is required for its ligase activity remains elusive. Here, we report the cryo-EM structure of the dimeric CRL3
Identifiants
pubmed: 38710693
doi: 10.1038/s41467-024-48045-2
pii: 10.1038/s41467-024-48045-2
doi:
Substances chimiques
Cullin Proteins
0
CUL3 protein, human
0
Ubiquitin-Protein Ligases
EC 2.3.2.27
IL17RB protein, human
0
Receptors, Interleukin-17
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
3789Subventions
Organisme : National Natural Science Foundation of China (National Science Foundation of China)
ID : 82030081
Organisme : National Natural Science Foundation of China (National Science Foundation of China)
ID : 81874235
Organisme : National Natural Science Foundation of China (National Science Foundation of China)
ID : 31800626
Organisme : National Natural Science Foundation of China (National Science Foundation of China)
ID : 32171224
Informations de copyright
© 2024. The Author(s).
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