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Resolving the Role of Actoymyosin Contractility in Cell Microrheology
Einstein's original description of Brownian motion established a direct relationship between thermally-excited random forces and the transport properties of a submicron particle in a viscous liquid. Recent work based on reconstituted actin filament networks suggests that nonthermal forces drive...
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Formato: | Texto |
Lenguaje: | English |
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Public Library of Science
2009
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2737638/ https://www.ncbi.nlm.nih.gov/pubmed/19756147 http://dx.doi.org/10.1371/journal.pone.0007054 |
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author | Hale, Christopher M. Sun, Sean X. Wirtz, Denis |
author_facet | Hale, Christopher M. Sun, Sean X. Wirtz, Denis |
author_sort | Hale, Christopher M. |
collection | PubMed |
description | Einstein's original description of Brownian motion established a direct relationship between thermally-excited random forces and the transport properties of a submicron particle in a viscous liquid. Recent work based on reconstituted actin filament networks suggests that nonthermal forces driven by the motor protein myosin II can induce large non-equilibrium fluctuations that dominate the motion of particles in cytoskeletal networks. Here, using high-resolution particle tracking, we find that thermal forces, not myosin-induced fluctuating forces, drive the motion of submicron particles embedded in the cytoskeleton of living cells. These results resolve the roles of myosin II and contractile actomyosin structures in the motion of nanoparticles lodged in the cytoplasm, reveal the biphasic mechanical architecture of adherent cells—stiff contractile stress fibers interdigitating in a network at the cell cortex and a soft actin meshwork in the body of the cell, validate the method of particle tracking-microrheology, and reconcile seemingly disparate atomic force microscopy (AFM) and particle-tracking microrheology measurements of living cells. |
format | Text |
id | pubmed-2737638 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2009 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-27376382009-09-16 Resolving the Role of Actoymyosin Contractility in Cell Microrheology Hale, Christopher M. Sun, Sean X. Wirtz, Denis PLoS One Research Article Einstein's original description of Brownian motion established a direct relationship between thermally-excited random forces and the transport properties of a submicron particle in a viscous liquid. Recent work based on reconstituted actin filament networks suggests that nonthermal forces driven by the motor protein myosin II can induce large non-equilibrium fluctuations that dominate the motion of particles in cytoskeletal networks. Here, using high-resolution particle tracking, we find that thermal forces, not myosin-induced fluctuating forces, drive the motion of submicron particles embedded in the cytoskeleton of living cells. These results resolve the roles of myosin II and contractile actomyosin structures in the motion of nanoparticles lodged in the cytoplasm, reveal the biphasic mechanical architecture of adherent cells—stiff contractile stress fibers interdigitating in a network at the cell cortex and a soft actin meshwork in the body of the cell, validate the method of particle tracking-microrheology, and reconcile seemingly disparate atomic force microscopy (AFM) and particle-tracking microrheology measurements of living cells. Public Library of Science 2009-09-16 /pmc/articles/PMC2737638/ /pubmed/19756147 http://dx.doi.org/10.1371/journal.pone.0007054 Text en Hale et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Hale, Christopher M. Sun, Sean X. Wirtz, Denis Resolving the Role of Actoymyosin Contractility in Cell Microrheology |
title | Resolving the Role of Actoymyosin Contractility in Cell Microrheology |
title_full | Resolving the Role of Actoymyosin Contractility in Cell Microrheology |
title_fullStr | Resolving the Role of Actoymyosin Contractility in Cell Microrheology |
title_full_unstemmed | Resolving the Role of Actoymyosin Contractility in Cell Microrheology |
title_short | Resolving the Role of Actoymyosin Contractility in Cell Microrheology |
title_sort | resolving the role of actoymyosin contractility in cell microrheology |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2737638/ https://www.ncbi.nlm.nih.gov/pubmed/19756147 http://dx.doi.org/10.1371/journal.pone.0007054 |
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