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Actin cable distribution and dynamics arising from cross-linking, motor pulling, and filament turnover
The growth of fission yeast relies on the polymerization of actin filaments nucleated by formin For3p, which localizes at tip cortical sites. These actin filaments bundle to form actin cables that span the cell and guide the movement of vesicles toward the cell tips. A big challenge is to develop a...
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/PMC4230589/ https://www.ncbi.nlm.nih.gov/pubmed/25103242 http://dx.doi.org/10.1091/mbc.E14-05-0965 |
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author | Tang, Haosu Laporte, Damien Vavylonis, Dimitrios |
author_facet | Tang, Haosu Laporte, Damien Vavylonis, Dimitrios |
author_sort | Tang, Haosu |
collection | PubMed |
description | The growth of fission yeast relies on the polymerization of actin filaments nucleated by formin For3p, which localizes at tip cortical sites. These actin filaments bundle to form actin cables that span the cell and guide the movement of vesicles toward the cell tips. A big challenge is to develop a quantitative understanding of these cellular actin structures. We used computer simulations to study the spatial and dynamical properties of actin cables. We simulated individual actin filaments as semiflexible polymers in three dimensions composed of beads connected with springs. Polymerization out of For3p cortical sites, bundling by cross-linkers, pulling by type V myosin, and severing by cofilin are simulated as growth, cross-linking, pulling, and turnover of the semiflexible polymers. With the foregoing mechanisms, the model generates actin cable structures and dynamics similar to those observed in live-cell experiments. Our simulations reproduce the particular actin cable structures in myoVΔ cells and predict the effect of increased myosin V pulling. Increasing cross-linking parameters generates thicker actin cables. It also leads to antiparallel and parallel phases with straight or curved cables, consistent with observations of cells overexpressing α-actinin. Finally, the model predicts that clustering of formins at cell tips promotes actin cable formation. |
format | Online Article Text |
id | pubmed-4230589 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-42305892014-12-16 Actin cable distribution and dynamics arising from cross-linking, motor pulling, and filament turnover Tang, Haosu Laporte, Damien Vavylonis, Dimitrios Mol Biol Cell Articles The growth of fission yeast relies on the polymerization of actin filaments nucleated by formin For3p, which localizes at tip cortical sites. These actin filaments bundle to form actin cables that span the cell and guide the movement of vesicles toward the cell tips. A big challenge is to develop a quantitative understanding of these cellular actin structures. We used computer simulations to study the spatial and dynamical properties of actin cables. We simulated individual actin filaments as semiflexible polymers in three dimensions composed of beads connected with springs. Polymerization out of For3p cortical sites, bundling by cross-linkers, pulling by type V myosin, and severing by cofilin are simulated as growth, cross-linking, pulling, and turnover of the semiflexible polymers. With the foregoing mechanisms, the model generates actin cable structures and dynamics similar to those observed in live-cell experiments. Our simulations reproduce the particular actin cable structures in myoVΔ cells and predict the effect of increased myosin V pulling. Increasing cross-linking parameters generates thicker actin cables. It also leads to antiparallel and parallel phases with straight or curved cables, consistent with observations of cells overexpressing α-actinin. Finally, the model predicts that clustering of formins at cell tips promotes actin cable formation. The American Society for Cell Biology 2014-10-01 /pmc/articles/PMC4230589/ /pubmed/25103242 http://dx.doi.org/10.1091/mbc.E14-05-0965 Text en © 2014 Tang 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 Tang, Haosu Laporte, Damien Vavylonis, Dimitrios Actin cable distribution and dynamics arising from cross-linking, motor pulling, and filament turnover |
title | Actin cable distribution and dynamics arising from cross-linking, motor pulling, and filament turnover |
title_full | Actin cable distribution and dynamics arising from cross-linking, motor pulling, and filament turnover |
title_fullStr | Actin cable distribution and dynamics arising from cross-linking, motor pulling, and filament turnover |
title_full_unstemmed | Actin cable distribution and dynamics arising from cross-linking, motor pulling, and filament turnover |
title_short | Actin cable distribution and dynamics arising from cross-linking, motor pulling, and filament turnover |
title_sort | actin cable distribution and dynamics arising from cross-linking, motor pulling, and filament turnover |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4230589/ https://www.ncbi.nlm.nih.gov/pubmed/25103242 http://dx.doi.org/10.1091/mbc.E14-05-0965 |
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