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Charge-dependent interactions of monomeric and filamentous actin with lipid bilayers
The cytoskeletal protein actin polymerizes into filaments that are essential for the mechanical stability of mammalian cells. In vitro experiments showed that direct interactions between actin filaments and lipid bilayers are possible and that the net charge of the bilayer as well as the presence of...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
National Academy of Sciences
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7084070/ https://www.ncbi.nlm.nih.gov/pubmed/32123101 http://dx.doi.org/10.1073/pnas.1914884117 |
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author | Schroer, Carsten F. E. Baldauf, Lucia van Buren, Lennard Wassenaar, Tsjerk A. Melo, Manuel N. Koenderink, Gijsje H. Marrink, Siewert J. |
author_facet | Schroer, Carsten F. E. Baldauf, Lucia van Buren, Lennard Wassenaar, Tsjerk A. Melo, Manuel N. Koenderink, Gijsje H. Marrink, Siewert J. |
author_sort | Schroer, Carsten F. E. |
collection | PubMed |
description | The cytoskeletal protein actin polymerizes into filaments that are essential for the mechanical stability of mammalian cells. In vitro experiments showed that direct interactions between actin filaments and lipid bilayers are possible and that the net charge of the bilayer as well as the presence of divalent ions in the buffer play an important role. In vivo, colocalization of actin filaments and divalent ions are suppressed, and cells rely on linker proteins to connect the plasma membrane to the actin network. Little is known, however, about why this is the case and what microscopic interactions are important. A deeper understanding is highly beneficial, first, to obtain understanding in the biological design of cells and, second, as a possible basis for the building of artificial cortices for the stabilization of synthetic cells. Here, we report the results of coarse-grained molecular dynamics simulations of monomeric and filamentous actin in the vicinity of differently charged lipid bilayers. We observe that charges on the lipid head groups strongly determine the ability of actin to adsorb to the bilayer. The inclusion of divalent ions leads to a reversal of the binding affinity. Our in silico results are validated experimentally by reconstitution assays with actin on lipid bilayer membranes and provide a molecular-level understanding of the actin–membrane interaction. |
format | Online Article Text |
id | pubmed-7084070 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | National Academy of Sciences |
record_format | MEDLINE/PubMed |
spelling | pubmed-70840702020-03-24 Charge-dependent interactions of monomeric and filamentous actin with lipid bilayers Schroer, Carsten F. E. Baldauf, Lucia van Buren, Lennard Wassenaar, Tsjerk A. Melo, Manuel N. Koenderink, Gijsje H. Marrink, Siewert J. Proc Natl Acad Sci U S A Biological Sciences The cytoskeletal protein actin polymerizes into filaments that are essential for the mechanical stability of mammalian cells. In vitro experiments showed that direct interactions between actin filaments and lipid bilayers are possible and that the net charge of the bilayer as well as the presence of divalent ions in the buffer play an important role. In vivo, colocalization of actin filaments and divalent ions are suppressed, and cells rely on linker proteins to connect the plasma membrane to the actin network. Little is known, however, about why this is the case and what microscopic interactions are important. A deeper understanding is highly beneficial, first, to obtain understanding in the biological design of cells and, second, as a possible basis for the building of artificial cortices for the stabilization of synthetic cells. Here, we report the results of coarse-grained molecular dynamics simulations of monomeric and filamentous actin in the vicinity of differently charged lipid bilayers. We observe that charges on the lipid head groups strongly determine the ability of actin to adsorb to the bilayer. The inclusion of divalent ions leads to a reversal of the binding affinity. Our in silico results are validated experimentally by reconstitution assays with actin on lipid bilayer membranes and provide a molecular-level understanding of the actin–membrane interaction. National Academy of Sciences 2020-03-17 2020-03-02 /pmc/articles/PMC7084070/ /pubmed/32123101 http://dx.doi.org/10.1073/pnas.1914884117 Text en Copyright © 2020 the Author(s). Published by PNAS. https://creativecommons.org/licenses/by-nc-nd/4.0/ https://creativecommons.org/licenses/by-nc-nd/4.0/This open access article is distributed under Creative Commons Attribution-NonCommercial-NoDerivatives License 4.0 (CC BY-NC-ND) (https://creativecommons.org/licenses/by-nc-nd/4.0/) . |
spellingShingle | Biological Sciences Schroer, Carsten F. E. Baldauf, Lucia van Buren, Lennard Wassenaar, Tsjerk A. Melo, Manuel N. Koenderink, Gijsje H. Marrink, Siewert J. Charge-dependent interactions of monomeric and filamentous actin with lipid bilayers |
title | Charge-dependent interactions of monomeric and filamentous actin with lipid bilayers |
title_full | Charge-dependent interactions of monomeric and filamentous actin with lipid bilayers |
title_fullStr | Charge-dependent interactions of monomeric and filamentous actin with lipid bilayers |
title_full_unstemmed | Charge-dependent interactions of monomeric and filamentous actin with lipid bilayers |
title_short | Charge-dependent interactions of monomeric and filamentous actin with lipid bilayers |
title_sort | charge-dependent interactions of monomeric and filamentous actin with lipid bilayers |
topic | Biological Sciences |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7084070/ https://www.ncbi.nlm.nih.gov/pubmed/32123101 http://dx.doi.org/10.1073/pnas.1914884117 |
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