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Myosin Vs organize actin cables in fission yeast
Myosin V motors are believed to contribute to cell polarization by carrying cargoes along actin tracks. In Schizosaccharomyces pombe, Myosin Vs transport secretory vesicles along actin cables, which are dynamic actin bundles assembled by the formin For3 at cell poles. How these flexible structures a...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3510019/ https://www.ncbi.nlm.nih.gov/pubmed/23051734 http://dx.doi.org/10.1091/mbc.E12-07-0499 |
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author | Lo Presti, Libera Chang, Fred Martin, Sophie G. |
author_facet | Lo Presti, Libera Chang, Fred Martin, Sophie G. |
author_sort | Lo Presti, Libera |
collection | PubMed |
description | Myosin V motors are believed to contribute to cell polarization by carrying cargoes along actin tracks. In Schizosaccharomyces pombe, Myosin Vs transport secretory vesicles along actin cables, which are dynamic actin bundles assembled by the formin For3 at cell poles. How these flexible structures are able to extend longitudinally in the cell through the dense cytoplasm is unknown. Here we show that in myosin V (myo52 myo51) null cells, actin cables are curled, bundled, and fail to extend into the cell interior. They also exhibit reduced retrograde flow, suggesting that formin-mediated actin assembly is impaired. Myo52 may contribute to actin cable organization by delivering actin regulators to cell poles, as myoV∆ defects are partially suppressed by diverting cargoes toward cell tips onto microtubules with a kinesin 7–Myo52 tail chimera. In addition, Myo52 motor activity may pull on cables to provide the tension necessary for their extension and efficient assembly, as artificially tethering actin cables to the nuclear envelope via a Myo52 motor domain restores actin cable extension and retrograde flow in myoV mutants. Together these in vivo data reveal elements of a self-organizing system in which the motors shape their own tracks by transporting cargoes and exerting physical pulling forces. |
format | Online Article Text |
id | pubmed-3510019 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-35100192013-02-16 Myosin Vs organize actin cables in fission yeast Lo Presti, Libera Chang, Fred Martin, Sophie G. Mol Biol Cell Articles Myosin V motors are believed to contribute to cell polarization by carrying cargoes along actin tracks. In Schizosaccharomyces pombe, Myosin Vs transport secretory vesicles along actin cables, which are dynamic actin bundles assembled by the formin For3 at cell poles. How these flexible structures are able to extend longitudinally in the cell through the dense cytoplasm is unknown. Here we show that in myosin V (myo52 myo51) null cells, actin cables are curled, bundled, and fail to extend into the cell interior. They also exhibit reduced retrograde flow, suggesting that formin-mediated actin assembly is impaired. Myo52 may contribute to actin cable organization by delivering actin regulators to cell poles, as myoV∆ defects are partially suppressed by diverting cargoes toward cell tips onto microtubules with a kinesin 7–Myo52 tail chimera. In addition, Myo52 motor activity may pull on cables to provide the tension necessary for their extension and efficient assembly, as artificially tethering actin cables to the nuclear envelope via a Myo52 motor domain restores actin cable extension and retrograde flow in myoV mutants. Together these in vivo data reveal elements of a self-organizing system in which the motors shape their own tracks by transporting cargoes and exerting physical pulling forces. The American Society for Cell Biology 2012-12-01 /pmc/articles/PMC3510019/ /pubmed/23051734 http://dx.doi.org/10.1091/mbc.E12-07-0499 Text en © 2012 Lo Presti 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 Lo Presti, Libera Chang, Fred Martin, Sophie G. Myosin Vs organize actin cables in fission yeast |
title | Myosin Vs organize actin cables in fission yeast |
title_full | Myosin Vs organize actin cables in fission yeast |
title_fullStr | Myosin Vs organize actin cables in fission yeast |
title_full_unstemmed | Myosin Vs organize actin cables in fission yeast |
title_short | Myosin Vs organize actin cables in fission yeast |
title_sort | myosin vs organize actin cables in fission yeast |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3510019/ https://www.ncbi.nlm.nih.gov/pubmed/23051734 http://dx.doi.org/10.1091/mbc.E12-07-0499 |
work_keys_str_mv | AT loprestilibera myosinvsorganizeactincablesinfissionyeast AT changfred myosinvsorganizeactincablesinfissionyeast AT martinsophieg myosinvsorganizeactincablesinfissionyeast |