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Cdc42 controls the dilation of the exocytotic fusion pore by regulating membrane tension
Membrane fusion underlies multiple processes, including exocytosis of hormones and neurotransmitters. Membrane fusion starts with the formation of a narrow fusion pore. Radial expansion of this pore completes the process and allows fast release of secretory compounds, but this step remains poorly un...
Autores principales: | , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4196869/ https://www.ncbi.nlm.nih.gov/pubmed/25143404 http://dx.doi.org/10.1091/mbc.E14-07-1229 |
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author | Bretou, Marine Jouannot, Ouardane Fanget, Isabelle Pierobon, Paolo Larochette, Nathanaël Gestraud, Pierre Guillon, Marc Emiliani, Valentina Gasman, Stéphane Desnos, Claire Lennon-Duménil, Ana-Maria Darchen, François |
author_facet | Bretou, Marine Jouannot, Ouardane Fanget, Isabelle Pierobon, Paolo Larochette, Nathanaël Gestraud, Pierre Guillon, Marc Emiliani, Valentina Gasman, Stéphane Desnos, Claire Lennon-Duménil, Ana-Maria Darchen, François |
author_sort | Bretou, Marine |
collection | PubMed |
description | Membrane fusion underlies multiple processes, including exocytosis of hormones and neurotransmitters. Membrane fusion starts with the formation of a narrow fusion pore. Radial expansion of this pore completes the process and allows fast release of secretory compounds, but this step remains poorly understood. Here we show that inhibiting the expression of the small GTPase Cdc42 or preventing its activation with a dominant negative Cdc42 construct in human neuroendocrine cells impaired the release process by compromising fusion pore enlargement. Consequently the mode of vesicle exocytosis was shifted from full-collapse fusion to kiss-and-run. Remarkably, Cdc42-knockdown cells showed reduced membrane tension, and the artificial increase of membrane tension restored fusion pore enlargement. Moreover, inhibiting the motor protein myosin II by blebbistatin decreased membrane tension, as well as fusion pore dilation. We conclude that membrane tension is the driving force for fusion pore dilation and that Cdc42 is a key regulator of this force. |
format | Online Article Text |
id | pubmed-4196869 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-41968692014-12-30 Cdc42 controls the dilation of the exocytotic fusion pore by regulating membrane tension Bretou, Marine Jouannot, Ouardane Fanget, Isabelle Pierobon, Paolo Larochette, Nathanaël Gestraud, Pierre Guillon, Marc Emiliani, Valentina Gasman, Stéphane Desnos, Claire Lennon-Duménil, Ana-Maria Darchen, François Mol Biol Cell Articles Membrane fusion underlies multiple processes, including exocytosis of hormones and neurotransmitters. Membrane fusion starts with the formation of a narrow fusion pore. Radial expansion of this pore completes the process and allows fast release of secretory compounds, but this step remains poorly understood. Here we show that inhibiting the expression of the small GTPase Cdc42 or preventing its activation with a dominant negative Cdc42 construct in human neuroendocrine cells impaired the release process by compromising fusion pore enlargement. Consequently the mode of vesicle exocytosis was shifted from full-collapse fusion to kiss-and-run. Remarkably, Cdc42-knockdown cells showed reduced membrane tension, and the artificial increase of membrane tension restored fusion pore enlargement. Moreover, inhibiting the motor protein myosin II by blebbistatin decreased membrane tension, as well as fusion pore dilation. We conclude that membrane tension is the driving force for fusion pore dilation and that Cdc42 is a key regulator of this force. The American Society for Cell Biology 2014-10-15 /pmc/articles/PMC4196869/ /pubmed/25143404 http://dx.doi.org/10.1091/mbc.E14-07-1229 Text en © 2014 Bretou, Jouannot, Fanget, et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society of Cell Biology. |
spellingShingle | Articles Bretou, Marine Jouannot, Ouardane Fanget, Isabelle Pierobon, Paolo Larochette, Nathanaël Gestraud, Pierre Guillon, Marc Emiliani, Valentina Gasman, Stéphane Desnos, Claire Lennon-Duménil, Ana-Maria Darchen, François Cdc42 controls the dilation of the exocytotic fusion pore by regulating membrane tension |
title | Cdc42 controls the dilation of the exocytotic fusion pore by regulating membrane tension |
title_full | Cdc42 controls the dilation of the exocytotic fusion pore by regulating membrane tension |
title_fullStr | Cdc42 controls the dilation of the exocytotic fusion pore by regulating membrane tension |
title_full_unstemmed | Cdc42 controls the dilation of the exocytotic fusion pore by regulating membrane tension |
title_short | Cdc42 controls the dilation of the exocytotic fusion pore by regulating membrane tension |
title_sort | cdc42 controls the dilation of the exocytotic fusion pore by regulating membrane tension |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4196869/ https://www.ncbi.nlm.nih.gov/pubmed/25143404 http://dx.doi.org/10.1091/mbc.E14-07-1229 |
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