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The beginning and the end of SNARE‐induced membrane fusion

Membrane fusion is not a spontaneous process. Physiologically, the formation of coiled‐coil protein complexes, the SNAREpins, bridges the membrane of a vesicle and a target membrane, brings them in close contact, and provides the energy necessary for their fusion. In this review, we utilize results...

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Autores principales: Mion, Delphine, Bunel, Louis, Heo, Paul, Pincet, Frédéric
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9623537/
https://www.ncbi.nlm.nih.gov/pubmed/35622519
http://dx.doi.org/10.1002/2211-5463.13447
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author Mion, Delphine
Bunel, Louis
Heo, Paul
Pincet, Frédéric
author_facet Mion, Delphine
Bunel, Louis
Heo, Paul
Pincet, Frédéric
author_sort Mion, Delphine
collection PubMed
description Membrane fusion is not a spontaneous process. Physiologically, the formation of coiled‐coil protein complexes, the SNAREpins, bridges the membrane of a vesicle and a target membrane, brings them in close contact, and provides the energy necessary for their fusion. In this review, we utilize results from in vitro experiments and simple physics and chemistry models to dissect the kinetics and energetics of the fusion process from the encounter of the two membranes to the full expansion of a fusion pore. We find three main energy barriers that oppose the fusion process: SNAREpin initiation, fusion pore opening, and expansion. SNAREpin initiation is inherent to the proteins and makes in vitro fusion kinetic experiments rather slow. The kinetics are physiologically accelerated by effectors. The energy barriers that precede pore opening and pore expansion can be overcome by several SNAREpins acting in concert.
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spelling pubmed-96235372022-11-02 The beginning and the end of SNARE‐induced membrane fusion Mion, Delphine Bunel, Louis Heo, Paul Pincet, Frédéric FEBS Open Bio Reviews Membrane fusion is not a spontaneous process. Physiologically, the formation of coiled‐coil protein complexes, the SNAREpins, bridges the membrane of a vesicle and a target membrane, brings them in close contact, and provides the energy necessary for their fusion. In this review, we utilize results from in vitro experiments and simple physics and chemistry models to dissect the kinetics and energetics of the fusion process from the encounter of the two membranes to the full expansion of a fusion pore. We find three main energy barriers that oppose the fusion process: SNAREpin initiation, fusion pore opening, and expansion. SNAREpin initiation is inherent to the proteins and makes in vitro fusion kinetic experiments rather slow. The kinetics are physiologically accelerated by effectors. The energy barriers that precede pore opening and pore expansion can be overcome by several SNAREpins acting in concert. John Wiley and Sons Inc. 2022-06-28 /pmc/articles/PMC9623537/ /pubmed/35622519 http://dx.doi.org/10.1002/2211-5463.13447 Text en © 2022 The Authors. FEBS Open Bio published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies. https://creativecommons.org/licenses/by/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Reviews
Mion, Delphine
Bunel, Louis
Heo, Paul
Pincet, Frédéric
The beginning and the end of SNARE‐induced membrane fusion
title The beginning and the end of SNARE‐induced membrane fusion
title_full The beginning and the end of SNARE‐induced membrane fusion
title_fullStr The beginning and the end of SNARE‐induced membrane fusion
title_full_unstemmed The beginning and the end of SNARE‐induced membrane fusion
title_short The beginning and the end of SNARE‐induced membrane fusion
title_sort beginning and the end of snare‐induced membrane fusion
topic Reviews
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9623537/
https://www.ncbi.nlm.nih.gov/pubmed/35622519
http://dx.doi.org/10.1002/2211-5463.13447
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