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Membrane fission by dynamin: what we know and what we need to know
The large GTPase dynamin is the first protein shown to catalyze membrane fission. Dynamin and its related proteins are essential to many cell functions, from endocytosis to organelle division and fusion, and it plays a critical role in many physiological functions such as synaptic transmission and m...
Autores principales: | , , , , , , , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5090216/ https://www.ncbi.nlm.nih.gov/pubmed/27670760 http://dx.doi.org/10.15252/embj.201694613 |
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author | Antonny, Bruno Burd, Christopher De Camilli, Pietro Chen, Elizabeth Daumke, Oliver Faelber, Katja Ford, Marijn Frolov, Vadim A Frost, Adam Hinshaw, Jenny E Kirchhausen, Tom Kozlov, Michael M Lenz, Martin Low, Harry H McMahon, Harvey Merrifield, Christien Pollard, Thomas D Robinson, Phillip J Roux, Aurélien Schmid, Sandra |
author_facet | Antonny, Bruno Burd, Christopher De Camilli, Pietro Chen, Elizabeth Daumke, Oliver Faelber, Katja Ford, Marijn Frolov, Vadim A Frost, Adam Hinshaw, Jenny E Kirchhausen, Tom Kozlov, Michael M Lenz, Martin Low, Harry H McMahon, Harvey Merrifield, Christien Pollard, Thomas D Robinson, Phillip J Roux, Aurélien Schmid, Sandra |
author_sort | Antonny, Bruno |
collection | PubMed |
description | The large GTPase dynamin is the first protein shown to catalyze membrane fission. Dynamin and its related proteins are essential to many cell functions, from endocytosis to organelle division and fusion, and it plays a critical role in many physiological functions such as synaptic transmission and muscle contraction. Research of the past three decades has focused on understanding how dynamin works. In this review, we present the basis for an emerging consensus on how dynamin functions. Three properties of dynamin are strongly supported by experimental data: first, dynamin oligomerizes into a helical polymer; second, dynamin oligomer constricts in the presence of GTP; and third, dynamin catalyzes membrane fission upon GTP hydrolysis. We present the two current models for fission, essentially diverging in how GTP energy is spent. We further discuss how future research might solve the remaining open questions presently under discussion. |
format | Online Article Text |
id | pubmed-5090216 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-50902162016-11-08 Membrane fission by dynamin: what we know and what we need to know Antonny, Bruno Burd, Christopher De Camilli, Pietro Chen, Elizabeth Daumke, Oliver Faelber, Katja Ford, Marijn Frolov, Vadim A Frost, Adam Hinshaw, Jenny E Kirchhausen, Tom Kozlov, Michael M Lenz, Martin Low, Harry H McMahon, Harvey Merrifield, Christien Pollard, Thomas D Robinson, Phillip J Roux, Aurélien Schmid, Sandra EMBO J Review The large GTPase dynamin is the first protein shown to catalyze membrane fission. Dynamin and its related proteins are essential to many cell functions, from endocytosis to organelle division and fusion, and it plays a critical role in many physiological functions such as synaptic transmission and muscle contraction. Research of the past three decades has focused on understanding how dynamin works. In this review, we present the basis for an emerging consensus on how dynamin functions. Three properties of dynamin are strongly supported by experimental data: first, dynamin oligomerizes into a helical polymer; second, dynamin oligomer constricts in the presence of GTP; and third, dynamin catalyzes membrane fission upon GTP hydrolysis. We present the two current models for fission, essentially diverging in how GTP energy is spent. We further discuss how future research might solve the remaining open questions presently under discussion. John Wiley and Sons Inc. 2016-09-26 2016-11-02 /pmc/articles/PMC5090216/ /pubmed/27670760 http://dx.doi.org/10.15252/embj.201694613 Text en © 2016 The Authors. Published under the terms of the CC BY NC ND 4.0 license This is an open access article under the terms of the Creative Commons Attribution‐NonCommercial‐NoDerivs 4.0 (http://creativecommons.org/licenses/by-nc-nd/4.0/) License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non‐commercial and no modifications or adaptations are made. |
spellingShingle | Review Antonny, Bruno Burd, Christopher De Camilli, Pietro Chen, Elizabeth Daumke, Oliver Faelber, Katja Ford, Marijn Frolov, Vadim A Frost, Adam Hinshaw, Jenny E Kirchhausen, Tom Kozlov, Michael M Lenz, Martin Low, Harry H McMahon, Harvey Merrifield, Christien Pollard, Thomas D Robinson, Phillip J Roux, Aurélien Schmid, Sandra Membrane fission by dynamin: what we know and what we need to know |
title | Membrane fission by dynamin: what we know and what we need to know |
title_full | Membrane fission by dynamin: what we know and what we need to know |
title_fullStr | Membrane fission by dynamin: what we know and what we need to know |
title_full_unstemmed | Membrane fission by dynamin: what we know and what we need to know |
title_short | Membrane fission by dynamin: what we know and what we need to know |
title_sort | membrane fission by dynamin: what we know and what we need to know |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5090216/ https://www.ncbi.nlm.nih.gov/pubmed/27670760 http://dx.doi.org/10.15252/embj.201694613 |
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