Bipolar filaments of human nonmuscle myosin 2-A and 2-B have distinct motile and mechanical properties
Nonmusclemyosin 2 (NM-2) powers cell motility and tissue morphogenesis by assembling into bipolar filaments that interact with actin. Although the enzymatic properties of purified NM-2 motor fragments have been determined, the emergent properties of filament ensembles are unknown. Using single myosi...
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/PMC5829915/ https://www.ncbi.nlm.nih.gov/pubmed/29419377 http://dx.doi.org/10.7554/eLife.32871 |
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author | Melli, Luca Billington, Neil Sun, Sara A Bird, Jonathan E Nagy, Attila Friedman, Thomas B Takagi, Yasuharu Sellers, James R |
author_facet | Melli, Luca Billington, Neil Sun, Sara A Bird, Jonathan E Nagy, Attila Friedman, Thomas B Takagi, Yasuharu Sellers, James R |
author_sort | Melli, Luca |
collection | PubMed |
description | Nonmusclemyosin 2 (NM-2) powers cell motility and tissue morphogenesis by assembling into bipolar filaments that interact with actin. Although the enzymatic properties of purified NM-2 motor fragments have been determined, the emergent properties of filament ensembles are unknown. Using single myosin filament in vitro motility assays, we report fundamental differences in filaments formed of different NM-2 motors. Filaments consisting of NM2-B moved processively along actin, while under identical conditions, NM2-A filaments did not. By more closely mimicking the physiological milieu, either by increasing solution viscosity or by co-polymerization with NM2-B, NM2-A containing filaments moved processively. Our data demonstrate that both the kinetic and mechanical properties of these two myosins, in addition to the stochiometry of NM-2 subunits, can tune filament mechanical output. We propose altering NM-2 filament composition is a general cellular strategy for tailoring force production of filaments to specific functions, such as maintaining tension or remodeling actin. |
format | Online Article Text |
id | pubmed-5829915 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | eLife Sciences Publications, Ltd |
record_format | MEDLINE/PubMed |
spelling | pubmed-58299152018-03-05 Bipolar filaments of human nonmuscle myosin 2-A and 2-B have distinct motile and mechanical properties Melli, Luca Billington, Neil Sun, Sara A Bird, Jonathan E Nagy, Attila Friedman, Thomas B Takagi, Yasuharu Sellers, James R eLife Structural Biology and Molecular Biophysics Nonmusclemyosin 2 (NM-2) powers cell motility and tissue morphogenesis by assembling into bipolar filaments that interact with actin. Although the enzymatic properties of purified NM-2 motor fragments have been determined, the emergent properties of filament ensembles are unknown. Using single myosin filament in vitro motility assays, we report fundamental differences in filaments formed of different NM-2 motors. Filaments consisting of NM2-B moved processively along actin, while under identical conditions, NM2-A filaments did not. By more closely mimicking the physiological milieu, either by increasing solution viscosity or by co-polymerization with NM2-B, NM2-A containing filaments moved processively. Our data demonstrate that both the kinetic and mechanical properties of these two myosins, in addition to the stochiometry of NM-2 subunits, can tune filament mechanical output. We propose altering NM-2 filament composition is a general cellular strategy for tailoring force production of filaments to specific functions, such as maintaining tension or remodeling actin. eLife Sciences Publications, Ltd 2018-02-08 /pmc/articles/PMC5829915/ /pubmed/29419377 http://dx.doi.org/10.7554/eLife.32871 Text en http://creativecommons.org/publicdomain/zero/1.0/ http://creativecommons.org/publicdomain/zero/1.0/This is an open-access article, free of all copyright, and may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose. The work is made available under the Creative Commons CC0 public domain dedication (http://creativecommons.org/publicdomain/zero/1.0/) . |
spellingShingle | Structural Biology and Molecular Biophysics Melli, Luca Billington, Neil Sun, Sara A Bird, Jonathan E Nagy, Attila Friedman, Thomas B Takagi, Yasuharu Sellers, James R Bipolar filaments of human nonmuscle myosin 2-A and 2-B have distinct motile and mechanical properties |
title | Bipolar filaments of human nonmuscle myosin 2-A and 2-B have distinct motile and mechanical properties |
title_full | Bipolar filaments of human nonmuscle myosin 2-A and 2-B have distinct motile and mechanical properties |
title_fullStr | Bipolar filaments of human nonmuscle myosin 2-A and 2-B have distinct motile and mechanical properties |
title_full_unstemmed | Bipolar filaments of human nonmuscle myosin 2-A and 2-B have distinct motile and mechanical properties |
title_short | Bipolar filaments of human nonmuscle myosin 2-A and 2-B have distinct motile and mechanical properties |
title_sort | bipolar filaments of human nonmuscle myosin 2-a and 2-b have distinct motile and mechanical properties |
topic | Structural Biology and Molecular Biophysics |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5829915/ https://www.ncbi.nlm.nih.gov/pubmed/29419377 http://dx.doi.org/10.7554/eLife.32871 |
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