The biochemical composition of the actomyosin network sets the magnitude of cellular traction forces-Reference-Cited by-同舟云学术

The biochemical composition of the actomyosin network sets the magnitude of cellular traction forces

Published:2021-08-19 Issue:18 Volume:32 Page:1737-1748
ISSN:1059-1524
Container-title:Molecular Biology of the Cell
language:en
Short-container-title:MBoC

Author:

Kollimada Somanna¹,Senger Fabrice¹,Vignaud Timothée¹²,Théry Manuel¹³,Blanchoin Laurent¹³,Kurzawa Laëtitia¹

Affiliation:

1. Interdisciplinary Research Institute of Grenoble, Laboratoire de Physiologie Cellulaire & Végétale, CytoMorpho Lab, University of Grenoble-Alpes, CEA, CNRS, INRA, Grenoble, France

2. Clinique de chirurgie digestive et endocrinienne, Hôtel Dieu, Nantes, 44093, France

3. Institut de Recherche Saint Louis, U976 Human Immunology Pathophysiology Immunotherapy (HIPI), CytoMorpho Lab, University of Paris, INSERM, CEA, Paris, France

Abstract

The endogenous content of proteins associated with force production and the resultant traction forces were quantified in the same cells using a new traction force-microscopy assay. Focal adhesion size correlated with force in stationary cells. Relative numbers of motors and cross-linkers per actin required an optimum to maximize cell force production.

Publisher

American Society for Cell Biology (ASCB)

Subject

Cell Biology,Molecular Biology

Reference76 articles.

1. Principles of Actomyosin Regulation In Vivo

2. Comparative Dynamics of Retrograde Actin Flow and Focal Adhesions: Formation of Nascent Adhesions Triggers Transition from Fast to Slow Flow

3. Molecular motors robustly drive active gels to a critically connected state

4. Force and focal adhesion assembly: a close relationship studied using elastic micropatterned substrates

5. Reference-Free Traction Force Microscopy Platform Fabricated via Two-Photon Laser Scanning Lithography Enables Facile Measurement of Cell-Generated Forces

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