Turbocharging synaptic transmission.

Autor: Rothman JE; Nanobiology Institute and Department of Cell Biology, Yale University, New Haven, CT, USA., Grushin K; Nanobiology Institute and Department of Cell Biology, Yale University, New Haven, CT, USA., Bera M; Nanobiology Institute and Department of Cell Biology, Yale University, New Haven, CT, USA., Pincet F; Nanobiology Institute and Department of Cell Biology, Yale University, New Haven, CT, USA.; Laboratoire de Physique de l'Ecole Normale Supérieure, ENS, Université PSL, CNRS, Sorbonne Université, Université Paris Cité, Paris, France.
Jazyk: angličtina
Zdroj: FEBS letters [FEBS Lett] 2023 Sep; Vol. 597 (18), pp. 2233-2249. Date of Electronic Publication: 2023 Sep 07.
DOI: 10.1002/1873-3468.14718
Abstrakt: Evidence from biochemistry, genetics, and electron microscopy strongly supports the idea that a ring of Synaptotagmin is central to the clamping and release of synaptic vesicles (SVs) for synchronous neurotransmission. Recent direct measurements in cell-free systems suggest there are 12 SNAREpins in each ready-release vesicle, consisting of six peripheral and six central SNAREpins. The six central SNAREpins are directly bound to the Synaptotagmin ring, are directly released by Ca ++ , and they initially open the fusion pore. The six peripheral SNAREpins are indirectly bound to the ring, each linked to a central SNAREpin by a bridging molecule of Complexin. We suggest that the primary role of peripheral SNAREpins is to provide additional force to 'turbocharge' neurotransmitter release, explaining how it can occur much faster than other forms of membrane fusion. The SV protein Synaptophysin forms hexamers that bear two copies of the v-SNARE VAMP at each vertex, one likely assembling into a peripheral SNAREpin and the other into a central SNAREpin.
(© 2023 The Authors. FEBS Letters published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.)
Databáze: MEDLINE
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