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Article Dans Une Revue Proceedings of the National Academy of Sciences of the United States of America Année : 2023

Synaptophysin Chaperones the Assembly of 12 SNAREpins under each Ready-Release Vesicle

Manindra Bera
  • Fonction : Auteur
Abhijith Radhakrishnan
Jeff Coleman
R. Venkat K. Sundaram
Sathish Ramakrishnan
Frederic Pincet
James Rothman

Résumé

The synaptic vesicle protein Synaptophysin has long been known to form a complex with the v-SNARE 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 Synaptophysin functions as a Synaptophysin forms a hexameric complex containing 12 copies of the v-SNARE VAMP2. These v-SNAREs assemble into SNAREpins as ready-release vesicles are formed in a fullydefined cell-free system, and do so in two equal waves organized by oligomerization of the Ca ++ sensor Synaptotagmin. In the absence of Synaptophysin, two waves are also observed, but the number of SNAREpins in each varies widely. We suggest that a single Synaptophysin hexamer in each vesicle symmetrically organizes 6 pairs of peripheral and central SNAREpins, the latter being directly bound to the Synaptotagmin ring. This gives rise to the symmetrical ring-like arrangement of densities observed by cryo-EM tomography under each synaptic vesicle (1, 2).
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Dates et versions

hal-04265788 , version 1 (31-10-2023)

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Manindra Bera, Abhijith Radhakrishnan, Jeff Coleman, R. Venkat K. Sundaram, Sathish Ramakrishnan, et al.. Synaptophysin Chaperones the Assembly of 12 SNAREpins under each Ready-Release Vesicle. Proceedings of the National Academy of Sciences of the United States of America, 2023, 120 (45), ⟨10.1073/pnas.2311484120⟩. ⟨hal-04265788⟩
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