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Ezrin enrichment on curved membranes requires a specific conformation or interaction with a curvature-sensitive partner
One challenge in cell biology is to decipher the biophysical mechanisms governing protein enrichment on curved membranes and the resulting membrane deformation. The ERM protein ezrin is abundant and associated with cellular membranes that are flat, positively or negatively curved. Using in vitro and...
Autores principales: | , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
eLife Sciences Publications, Ltd
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6167055/ https://www.ncbi.nlm.nih.gov/pubmed/30234483 http://dx.doi.org/10.7554/eLife.37262 |
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author | Tsai, Feng-Ching Bertin, Aurelie Bousquet, Hugo Manzi, John Senju, Yosuke Tsai, Meng-Chen Picas, Laura Miserey-Lenkei, Stephanie Lappalainen, Pekka Lemichez, Emmanuel Coudrier, Evelyne Bassereau, Patricia |
author_facet | Tsai, Feng-Ching Bertin, Aurelie Bousquet, Hugo Manzi, John Senju, Yosuke Tsai, Meng-Chen Picas, Laura Miserey-Lenkei, Stephanie Lappalainen, Pekka Lemichez, Emmanuel Coudrier, Evelyne Bassereau, Patricia |
author_sort | Tsai, Feng-Ching |
collection | PubMed |
description | One challenge in cell biology is to decipher the biophysical mechanisms governing protein enrichment on curved membranes and the resulting membrane deformation. The ERM protein ezrin is abundant and associated with cellular membranes that are flat, positively or negatively curved. Using in vitro and cell biology approaches, we assess mechanisms of ezrin’s enrichment on curved membranes. We evidence that wild-type ezrin (ezrinWT) and its phosphomimetic mutant T567D (ezrinTD) do not deform membranes but self-assemble anti-parallelly, zipping adjacent membranes. EzrinTD’s specific conformation reduces intermolecular interactions, allows binding to actin filaments, which reduces membrane tethering, and promotes ezrin binding to positively-curved membranes. While neither ezrinTD nor ezrinWT senses negative curvature alone, we demonstrate that interacting with curvature-sensing I-BAR-domain proteins facilitates ezrin enrichment in negatively-curved membrane protrusions. Overall, our work demonstrates that ezrin can tether membranes, or be targeted to curved membranes, depending on conformations and interactions with actin and curvature-sensing binding partners. |
format | Online Article Text |
id | pubmed-6167055 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | eLife Sciences Publications, Ltd |
record_format | MEDLINE/PubMed |
spelling | pubmed-61670552018-10-02 Ezrin enrichment on curved membranes requires a specific conformation or interaction with a curvature-sensitive partner Tsai, Feng-Ching Bertin, Aurelie Bousquet, Hugo Manzi, John Senju, Yosuke Tsai, Meng-Chen Picas, Laura Miserey-Lenkei, Stephanie Lappalainen, Pekka Lemichez, Emmanuel Coudrier, Evelyne Bassereau, Patricia eLife Physics of Living Systems One challenge in cell biology is to decipher the biophysical mechanisms governing protein enrichment on curved membranes and the resulting membrane deformation. The ERM protein ezrin is abundant and associated with cellular membranes that are flat, positively or negatively curved. Using in vitro and cell biology approaches, we assess mechanisms of ezrin’s enrichment on curved membranes. We evidence that wild-type ezrin (ezrinWT) and its phosphomimetic mutant T567D (ezrinTD) do not deform membranes but self-assemble anti-parallelly, zipping adjacent membranes. EzrinTD’s specific conformation reduces intermolecular interactions, allows binding to actin filaments, which reduces membrane tethering, and promotes ezrin binding to positively-curved membranes. While neither ezrinTD nor ezrinWT senses negative curvature alone, we demonstrate that interacting with curvature-sensing I-BAR-domain proteins facilitates ezrin enrichment in negatively-curved membrane protrusions. Overall, our work demonstrates that ezrin can tether membranes, or be targeted to curved membranes, depending on conformations and interactions with actin and curvature-sensing binding partners. eLife Sciences Publications, Ltd 2018-09-20 /pmc/articles/PMC6167055/ /pubmed/30234483 http://dx.doi.org/10.7554/eLife.37262 Text en © 2018, Tsai et al http://creativecommons.org/licenses/by/4.0/ http://creativecommons.org/licenses/by/4.0/This article is distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use and redistribution provided that the original author and source are credited. |
spellingShingle | Physics of Living Systems Tsai, Feng-Ching Bertin, Aurelie Bousquet, Hugo Manzi, John Senju, Yosuke Tsai, Meng-Chen Picas, Laura Miserey-Lenkei, Stephanie Lappalainen, Pekka Lemichez, Emmanuel Coudrier, Evelyne Bassereau, Patricia Ezrin enrichment on curved membranes requires a specific conformation or interaction with a curvature-sensitive partner |
title | Ezrin enrichment on curved membranes requires a specific conformation or interaction with a curvature-sensitive partner |
title_full | Ezrin enrichment on curved membranes requires a specific conformation or interaction with a curvature-sensitive partner |
title_fullStr | Ezrin enrichment on curved membranes requires a specific conformation or interaction with a curvature-sensitive partner |
title_full_unstemmed | Ezrin enrichment on curved membranes requires a specific conformation or interaction with a curvature-sensitive partner |
title_short | Ezrin enrichment on curved membranes requires a specific conformation or interaction with a curvature-sensitive partner |
title_sort | ezrin enrichment on curved membranes requires a specific conformation or interaction with a curvature-sensitive partner |
topic | Physics of Living Systems |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6167055/ https://www.ncbi.nlm.nih.gov/pubmed/30234483 http://dx.doi.org/10.7554/eLife.37262 |
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