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F-actin bending facilitates net actomyosin contraction By inhibiting expansion with plus-end-located myosin motors
Contraction of actomyosin networks underpins important cellular processes including motility and division. The mechanical origin of actomyosin contraction is not fully-understood. We investigate whether contraction arises on the scale of individual filaments, without needing to invoke network-scale...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer Berlin Heidelberg
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9252981/ https://www.ncbi.nlm.nih.gov/pubmed/35788426 http://dx.doi.org/10.1007/s00285-022-01737-z |
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author | Tam, Alexander K. Y. Mogilner, Alex Oelz, Dietmar B. |
author_facet | Tam, Alexander K. Y. Mogilner, Alex Oelz, Dietmar B. |
author_sort | Tam, Alexander K. Y. |
collection | PubMed |
description | Contraction of actomyosin networks underpins important cellular processes including motility and division. The mechanical origin of actomyosin contraction is not fully-understood. We investigate whether contraction arises on the scale of individual filaments, without needing to invoke network-scale interactions. We derive discrete force-balance and continuum partial differential equations for two symmetric, semi-flexible actin filaments with an attached myosin motor. Assuming the system exists within a homogeneous background material, our method enables computation of the stress tensor, providing a measure of contractility. After deriving the model, we use a combination of asymptotic analysis and numerical solutions to show how F-actin bending facilitates contraction on the scale of two filaments. Rigid filaments exhibit polarity-reversal symmetry as the motor travels from the minus to plus-ends, such that contractile and expansive components cancel. Filament bending induces a geometric asymmetry that brings the filaments closer to parallel as a myosin motor approaches their plus-ends, decreasing the effective spring force opposing motor motion. The reduced spring force enables the motor to move faster close to filament plus-ends, which reduces expansive stress and gives rise to net contraction. Bending-induced geometric asymmetry provides both new understanding of actomyosin contraction mechanics, and a hypothesis that can be tested in experiments. |
format | Online Article Text |
id | pubmed-9252981 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Springer Berlin Heidelberg |
record_format | MEDLINE/PubMed |
spelling | pubmed-92529812022-07-06 F-actin bending facilitates net actomyosin contraction By inhibiting expansion with plus-end-located myosin motors Tam, Alexander K. Y. Mogilner, Alex Oelz, Dietmar B. J Math Biol Article Contraction of actomyosin networks underpins important cellular processes including motility and division. The mechanical origin of actomyosin contraction is not fully-understood. We investigate whether contraction arises on the scale of individual filaments, without needing to invoke network-scale interactions. We derive discrete force-balance and continuum partial differential equations for two symmetric, semi-flexible actin filaments with an attached myosin motor. Assuming the system exists within a homogeneous background material, our method enables computation of the stress tensor, providing a measure of contractility. After deriving the model, we use a combination of asymptotic analysis and numerical solutions to show how F-actin bending facilitates contraction on the scale of two filaments. Rigid filaments exhibit polarity-reversal symmetry as the motor travels from the minus to plus-ends, such that contractile and expansive components cancel. Filament bending induces a geometric asymmetry that brings the filaments closer to parallel as a myosin motor approaches their plus-ends, decreasing the effective spring force opposing motor motion. The reduced spring force enables the motor to move faster close to filament plus-ends, which reduces expansive stress and gives rise to net contraction. Bending-induced geometric asymmetry provides both new understanding of actomyosin contraction mechanics, and a hypothesis that can be tested in experiments. Springer Berlin Heidelberg 2022-07-04 2022 /pmc/articles/PMC9252981/ /pubmed/35788426 http://dx.doi.org/10.1007/s00285-022-01737-z Text en © The Author(s) 2022 https://creativecommons.org/licenses/by/4.0/Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Article Tam, Alexander K. Y. Mogilner, Alex Oelz, Dietmar B. F-actin bending facilitates net actomyosin contraction By inhibiting expansion with plus-end-located myosin motors |
title | F-actin bending facilitates net actomyosin contraction By inhibiting expansion with plus-end-located myosin motors |
title_full | F-actin bending facilitates net actomyosin contraction By inhibiting expansion with plus-end-located myosin motors |
title_fullStr | F-actin bending facilitates net actomyosin contraction By inhibiting expansion with plus-end-located myosin motors |
title_full_unstemmed | F-actin bending facilitates net actomyosin contraction By inhibiting expansion with plus-end-located myosin motors |
title_short | F-actin bending facilitates net actomyosin contraction By inhibiting expansion with plus-end-located myosin motors |
title_sort | f-actin bending facilitates net actomyosin contraction by inhibiting expansion with plus-end-located myosin motors |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9252981/ https://www.ncbi.nlm.nih.gov/pubmed/35788426 http://dx.doi.org/10.1007/s00285-022-01737-z |
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