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Local Monomer Levels and Established Filaments Potentiate Non-Muscle Myosin 2 Assembly
The ability to dynamically assemble contractile networks is required throughout cell physiology, yet the biophysical mechanisms regulating non-muscle myosin 2 filament assembly in living cells are lacking. Here we use a suite of dynamic, quantitative imaging approaches to identify deterministic fact...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Cold Spring Harbor Laboratory
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10168331/ https://www.ncbi.nlm.nih.gov/pubmed/37162845 http://dx.doi.org/10.1101/2023.04.26.538303 |
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author | Quintanilla, Melissa A. Patel, Hiral Wu, Huini Sochacki, Kem A. Akamatsu, Matthew Rotty, Jeremy D. Korobova, Farida Bear, James E. Taraska, Justin W. Oakes, Patrick W. Beach, Jordan R. |
author_facet | Quintanilla, Melissa A. Patel, Hiral Wu, Huini Sochacki, Kem A. Akamatsu, Matthew Rotty, Jeremy D. Korobova, Farida Bear, James E. Taraska, Justin W. Oakes, Patrick W. Beach, Jordan R. |
author_sort | Quintanilla, Melissa A. |
collection | PubMed |
description | The ability to dynamically assemble contractile networks is required throughout cell physiology, yet the biophysical mechanisms regulating non-muscle myosin 2 filament assembly in living cells are lacking. Here we use a suite of dynamic, quantitative imaging approaches to identify deterministic factors that drive myosin filament appearance and amplification. We find that actin dynamics regulate myosin assembly, but that the actin architecture plays a minimal direct role. Instead, remodeling of actin networks modulates the local myosin monomer levels and facilitates assembly through myosin:myosin driven interactions. Using optogenetically controlled myosin, we demonstrate that locally concentrating myosin is sufficient to both form filaments and jump-start filament amplification and partitioning. By counting myosin monomers within filaments, we demonstrate a myosin-facilitated assembly process that establishes sub-resolution filament stacks prior to partitioning into clusters that feed higher-order networks. Together these findings establish the biophysical mechanisms regulating the assembly of non-muscle contractile structures that are ubiquitous throughout cell biology. |
format | Online Article Text |
id | pubmed-10168331 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Cold Spring Harbor Laboratory |
record_format | MEDLINE/PubMed |
spelling | pubmed-101683312023-05-10 Local Monomer Levels and Established Filaments Potentiate Non-Muscle Myosin 2 Assembly Quintanilla, Melissa A. Patel, Hiral Wu, Huini Sochacki, Kem A. Akamatsu, Matthew Rotty, Jeremy D. Korobova, Farida Bear, James E. Taraska, Justin W. Oakes, Patrick W. Beach, Jordan R. bioRxiv Article The ability to dynamically assemble contractile networks is required throughout cell physiology, yet the biophysical mechanisms regulating non-muscle myosin 2 filament assembly in living cells are lacking. Here we use a suite of dynamic, quantitative imaging approaches to identify deterministic factors that drive myosin filament appearance and amplification. We find that actin dynamics regulate myosin assembly, but that the actin architecture plays a minimal direct role. Instead, remodeling of actin networks modulates the local myosin monomer levels and facilitates assembly through myosin:myosin driven interactions. Using optogenetically controlled myosin, we demonstrate that locally concentrating myosin is sufficient to both form filaments and jump-start filament amplification and partitioning. By counting myosin monomers within filaments, we demonstrate a myosin-facilitated assembly process that establishes sub-resolution filament stacks prior to partitioning into clusters that feed higher-order networks. Together these findings establish the biophysical mechanisms regulating the assembly of non-muscle contractile structures that are ubiquitous throughout cell biology. Cold Spring Harbor Laboratory 2023-04-27 /pmc/articles/PMC10168331/ /pubmed/37162845 http://dx.doi.org/10.1101/2023.04.26.538303 Text en https://creativecommons.org/licenses/by-nc-nd/4.0/This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License (https://creativecommons.org/licenses/by-nc-nd/4.0/) , which allows reusers to copy and distribute the material in any medium or format in unadapted form only, for noncommercial purposes only, and only so long as attribution is given to the creator. |
spellingShingle | Article Quintanilla, Melissa A. Patel, Hiral Wu, Huini Sochacki, Kem A. Akamatsu, Matthew Rotty, Jeremy D. Korobova, Farida Bear, James E. Taraska, Justin W. Oakes, Patrick W. Beach, Jordan R. Local Monomer Levels and Established Filaments Potentiate Non-Muscle Myosin 2 Assembly |
title | Local Monomer Levels and Established Filaments Potentiate Non-Muscle Myosin 2 Assembly |
title_full | Local Monomer Levels and Established Filaments Potentiate Non-Muscle Myosin 2 Assembly |
title_fullStr | Local Monomer Levels and Established Filaments Potentiate Non-Muscle Myosin 2 Assembly |
title_full_unstemmed | Local Monomer Levels and Established Filaments Potentiate Non-Muscle Myosin 2 Assembly |
title_short | Local Monomer Levels and Established Filaments Potentiate Non-Muscle Myosin 2 Assembly |
title_sort | local monomer levels and established filaments potentiate non-muscle myosin 2 assembly |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10168331/ https://www.ncbi.nlm.nih.gov/pubmed/37162845 http://dx.doi.org/10.1101/2023.04.26.538303 |
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