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...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Christopher M Hale, Sean X Sun, Denis Wirtz
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2009
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/04336d10358b429b8465cc8fce402f64
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:04336d10358b429b8465cc8fce402f64
record_format	dspace
spelling	oai:doaj.org-article:04336d10358b429b8465cc8fce402f642021-11-25T06:20:21ZResolving the role of actoymyosin contractility in cell microrheology.1932-620310.1371/journal.pone.0007054https://doaj.org/article/04336d10358b429b8465cc8fce402f642009-09-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/19756147/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203Einstein'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.Christopher M HaleSean X SunDenis WirtzPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 4, Iss 9, p e7054 (2009)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Christopher M Hale Sean X Sun Denis Wirtz Resolving the role of actoymyosin contractility in cell microrheology.
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	article
author	Christopher M Hale Sean X Sun Denis Wirtz
author_facet	Christopher M Hale Sean X Sun Denis Wirtz
author_sort	Christopher M Hale
title	Resolving the role of actoymyosin contractility in cell microrheology.
title_short	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_sort	resolving the role of actoymyosin contractility in cell microrheology.
publisher	Public Library of Science (PLoS)
publishDate	2009
url	https://doaj.org/article/04336d10358b429b8465cc8fce402f64
work_keys_str_mv	AT christophermhale resolvingtheroleofactoymyosincontractilityincellmicrorheology AT seanxsun resolvingtheroleofactoymyosincontractilityincellmicrorheology AT deniswirtz resolvingtheroleofactoymyosincontractilityincellmicrorheology
_version_	1718413782709960704

Resolving the role of actoymyosin contractility in cell microrheology.

Ejemplares similares