Study of the influence of actin-binding proteins using linear analyses of cell deformability

Plaza Baonza, Gustavo Ramón and Uyeda, Taro Q. P. and Mirzaei, Zahra and Simmons, Craig A. (2015). Study of the influence of actin-binding proteins using linear analyses of cell deformability. "Soft Matter", v. 11 (n. 27); pp. 5435-5446. ISSN 1744-683X. https://doi.org/10.1039/C5SM00125K.

Description

Title: Study of the influence of actin-binding proteins using linear analyses of cell deformability
Author/s:
  • Plaza Baonza, Gustavo Ramón
  • Uyeda, Taro Q. P.
  • Mirzaei, Zahra
  • Simmons, Craig A.
Item Type: Article
Título de Revista/Publicación: Soft Matter
Date: June 2015
ISSN: 1744-683X
Volume: 11
Subjects:
Faculty: E.T.S.I. Caminos, Canales y Puertos (UPM)
Department: Ciencia de los Materiales
Creative Commons Licenses: Recognition - No derivative works - Non commercial

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Abstract

The actin cytoskeleton plays a key role in the deformability of the cell and in mechanosensing. Here we analyze the contributions of three major actin cross-linking proteins, myosin II, a-actinin and filamin, to cell deformability, by using micropipette aspiration of Dictyostelium cells. We examine the applicability of three simple mechanical models: for small deformation, linear viscoelasticity and drop of liquid with a tense cortex; and for large deformation, a Newtonian viscous fluid. For these models, we have derived linearized equations and we provide a novel, straightforward methodology to analyze the experiments. This methodology allowed us to differentiate the effects of the cross-linking proteins in the different regimes of deformation. Our results confirm some previous observations and suggest important relations between the molecular characteristics of the actin-binding proteins and the cell behavior: the effect of myosin is explained in terms of the relation between the lifetime of the bond to actin and the resistive force; the presence of a-actinin obstructs the deformation of the cytoskeleton, presumably mainly due to the higher molecular stiffness and to the lower dissociation rate constants; and filamin contributes critically to the global connectivity of the network, possibly by rapidly turning over crosslinks during the remodeling of the cytoskeletal network, thanks to the higher rate constants, flexibility and larger size. The results suggest a sophisticated relationship between the expression levels of actinbinding proteins, deformability and mechanosensing.

More information

Item ID: 41172
DC Identifier: http://oa.upm.es/41172/
OAI Identifier: oai:oa.upm.es:41172
DOI: 10.1039/C5SM00125K
Official URL: http://pubs.rsc.org/en/content/articlelanding/2015/sm/c5sm00125k#!divAbstract
Deposited by: Memoria Investigacion
Deposited on: 23 Jun 2016 15:30
Last Modified: 23 Jun 2016 15:30
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