Architecture of the ESCPE-1 membrane coat.
Journal
Nature structural & molecular biology
ISSN: 1545-9985
Titre abrégé: Nat Struct Mol Biol
Pays: United States
ID NLM: 101186374
Informations de publication
Date de publication:
07 2023
07 2023
Historique:
received:
13
10
2022
accepted:
05
05
2023
medline:
19
7
2023
pubmed:
16
6
2023
entrez:
15
6
2023
Statut:
ppublish
Résumé
Recycling of membrane proteins enables the reuse of receptors, ion channels and transporters. A key component of the recycling machinery is the endosomal sorting complex for promoting exit 1 (ESCPE-1), which rescues transmembrane proteins from the endolysosomal pathway for transport to the trans-Golgi network and the plasma membrane. This rescue entails the formation of recycling tubules through ESCPE-1 recruitment, cargo capture, coat assembly and membrane sculpting by mechanisms that remain largely unknown. Herein, we show that ESCPE-1 has a single-layer coat organization and suggest how synergistic interactions between ESCPE-1 protomers, phosphoinositides and cargo molecules result in a global arrangement of amphipathic helices to drive tubule formation. Our results thus define a key process of tubule-based endosomal sorting.
Identifiants
pubmed: 37322239
doi: 10.1038/s41594-023-01014-7
pii: 10.1038/s41594-023-01014-7
pmc: PMC10352136
doi:
Substances chimiques
Carrier Proteins
0
Membrane Proteins
0
Types de publication
Journal Article
Research Support, N.I.H., Intramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
958-969Subventions
Organisme : Intramural NIH HHS
ID : Z01 HD001607
Pays : United States
Organisme : Intramural NIH HHS
ID : ZIA HD001607
Pays : United States
Informations de copyright
© 2023. The Author(s).
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