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Actomyosin contractility and buckling of microtubules in nucleation, growth and disassembling of focal adhesions

Building up and maintenance of cytoskeletal structure in living cells are force-dependent processes involving a dynamic chain of polymerization and depolymerization events, which are also at the basis of cells’ remodelling and locomotion. All these phenomena develop by establishing cell–matrix inter...

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Autores principales: Palumbo, S., Benvenuti, E., Fraldi, M.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Berlin Heidelberg 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9283365/
https://www.ncbi.nlm.nih.gov/pubmed/35614374
http://dx.doi.org/10.1007/s10237-022-01584-3
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author Palumbo, S.
Benvenuti, E.
Fraldi, M.
author_facet Palumbo, S.
Benvenuti, E.
Fraldi, M.
author_sort Palumbo, S.
collection PubMed
description Building up and maintenance of cytoskeletal structure in living cells are force-dependent processes involving a dynamic chain of polymerization and depolymerization events, which are also at the basis of cells’ remodelling and locomotion. All these phenomena develop by establishing cell–matrix interfaces made of protein complexes, known as focal adhesions, which govern mechanosensing and mechanotransduction mechanisms mediated by stress transmission between cell interior and external environment. Within this framework, by starting from a work by Cao et al. (Biophys J 109:1807–1817, 2015), we here investigate the role played by actomyosin contractility of stress fibres in nucleation, growth and disassembling of focal adhesions. In particular, we propose a tensegrity model of an adherent cell incorporating nonlinear elasticity and unstable behaviours, which provides a new kinematical interpretation of cellular contractile forces and describes how stress fibres, microtubules and adhesion plaques interact mechanobiologically. The results confirm some experimental evidences and suggest how the actomyosin contraction level could be exploited by cells to actively control their adhesion, eventually triggering cytoskeleton reconfigurations and migration processes observed in both physiological conditions and diseases. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1007/s10237-022-01584-3.
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spelling pubmed-92833652022-07-16 Actomyosin contractility and buckling of microtubules in nucleation, growth and disassembling of focal adhesions Palumbo, S. Benvenuti, E. Fraldi, M. Biomech Model Mechanobiol Original Paper Building up and maintenance of cytoskeletal structure in living cells are force-dependent processes involving a dynamic chain of polymerization and depolymerization events, which are also at the basis of cells’ remodelling and locomotion. All these phenomena develop by establishing cell–matrix interfaces made of protein complexes, known as focal adhesions, which govern mechanosensing and mechanotransduction mechanisms mediated by stress transmission between cell interior and external environment. Within this framework, by starting from a work by Cao et al. (Biophys J 109:1807–1817, 2015), we here investigate the role played by actomyosin contractility of stress fibres in nucleation, growth and disassembling of focal adhesions. In particular, we propose a tensegrity model of an adherent cell incorporating nonlinear elasticity and unstable behaviours, which provides a new kinematical interpretation of cellular contractile forces and describes how stress fibres, microtubules and adhesion plaques interact mechanobiologically. The results confirm some experimental evidences and suggest how the actomyosin contraction level could be exploited by cells to actively control their adhesion, eventually triggering cytoskeleton reconfigurations and migration processes observed in both physiological conditions and diseases. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1007/s10237-022-01584-3. Springer Berlin Heidelberg 2022-05-25 2022 /pmc/articles/PMC9283365/ /pubmed/35614374 http://dx.doi.org/10.1007/s10237-022-01584-3 Text en © The Author(s) 2022, corrected publication 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 Original Paper
Palumbo, S.
Benvenuti, E.
Fraldi, M.
Actomyosin contractility and buckling of microtubules in nucleation, growth and disassembling of focal adhesions
title Actomyosin contractility and buckling of microtubules in nucleation, growth and disassembling of focal adhesions
title_full Actomyosin contractility and buckling of microtubules in nucleation, growth and disassembling of focal adhesions
title_fullStr Actomyosin contractility and buckling of microtubules in nucleation, growth and disassembling of focal adhesions
title_full_unstemmed Actomyosin contractility and buckling of microtubules in nucleation, growth and disassembling of focal adhesions
title_short Actomyosin contractility and buckling of microtubules in nucleation, growth and disassembling of focal adhesions
title_sort actomyosin contractility and buckling of microtubules in nucleation, growth and disassembling of focal adhesions
topic Original Paper
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9283365/
https://www.ncbi.nlm.nih.gov/pubmed/35614374
http://dx.doi.org/10.1007/s10237-022-01584-3
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