Synaptophysin chaperones the assembly of 12 SNAREpins under each ready-release vesicle.
SNAREpins
Synaptotagmin1
VAMP2
neurotransmitter release
synaptophysin
Journal
Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876
Informations de publication
Date de publication:
07 Nov 2023
07 Nov 2023
Historique:
medline:
1
11
2023
pubmed:
30
10
2023
entrez:
30
10
2023
Statut:
ppublish
Résumé
The synaptic vesicle protein Synaptophysin (Syp) has long been known to form a complex with the Vesicle associated soluble N-ethylmaleimide sensitive fusion protein attachment receptor (v-SNARE) Vesicle associated membrane protein (VAMP), but a more specific molecular function or mechanism of action in exocytosis has been lacking because gene knockouts have minimal effects. Utilizing fully defined reconstitution and single-molecule measurements, we now report that Syp functions as a chaperone that determines the number of SNAREpins assembling between a ready-release vesicle and its target membrane bilayer. Specifically, Syp directs the assembly of 12 ± 1 SNAREpins under each docked vesicle, even in the face of an excess of SNARE proteins. The SNAREpins assemble in successive waves of 6 ± 1 and 5 ± 2 SNAREpins, respectively, tightly linked to oligomerization of and binding to the vesicle Ca
Identifiants
pubmed: 37903271
doi: 10.1073/pnas.2311484120
pmc: PMC10636311
doi:
Substances chimiques
Synaptophysin
0
Synaptotagmins
134193-27-4
SNARE Proteins
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
e2311484120Commentaires et corrections
Type : UpdateOf
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