HAL will be down for maintenance from Friday, June 10 at 4pm through Monday, June 13 at 9am. More information
Skip to Main content Skip to Navigation
Journal articles

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

Abstract : The regulation of cellular force production relies on the complex interplay between a well-conserved set of proteins of the cytoskeleton: actin, myosin, and α-actinin. Despite our deep knowledge of the role of these proteins in force production at the molecular scale, our understanding of the biochemical regulation of the magnitude of traction forces generated at the entire-cell level has been limited, notably by the technical challenge of measuring traction forces and the endogenous biochemical composition in the same cell. In this study, we developed an alternative Traction-Force Microscopy (TFM) assay, which used a combination of hydrogel micropatterning to define cell adhesion and shape and an intermediate fixation/immunolabeling step to characterize strain energies and the endogenous protein contents in single epithelial cells. Our results demonstrated that both the signal intensity and the area of the Focal Adhesion (FA)–associated protein vinculin showed a strong positive correlation with strain energy in mature FAs. Individual contents from actin filament and phospho-myosin displayed broader deviation in their linear relationship to strain energies. Instead, our quantitative analyzes demonstrated that their relative amount exhibited an optimum ratio of phospho-myosin to actin, allowing maximum force production by cells. By contrast, although no correlation was identified between individual α-actinin content and strain energy, the ratio of α-actinin to actin filaments was inversely related to strain energy. Hence, our results suggest that, in the cellular model studied, traction-force magnitude is dictated by the relative numbers of molecular motors and cross-linkers per actin filament, rather than the amounts of an individual component in the cytoskeletal network. This assay offers new perspectives to study in more detail the complex interplay between the endogenous biochemical composition of individual cells and the force they produce.
Complete list of metadata

https://hal.archives-ouvertes.fr/hal-03366003
Contributor : Jacqueline Martin-Laffon Connect in order to contact the contributor
Submitted on : Tuesday, October 5, 2021 - 3:11:50 PM
Last modification on : Thursday, April 7, 2022 - 1:58:26 PM
Long-term archiving on: : Thursday, January 6, 2022 - 7:38:46 PM

File

Kollimada et al - Mol Biol. Ce...
Publisher files allowed on an open archive

Identifiers

Collections

Citation

Somanna Kollimada, Fabrice Senger, Timothée Vignaud, Manuel Théry, Laurent Blanchoin, et al.. The biochemical composition of the actomyosin network sets the magnitude of cellular traction forces. Molecular Biology of the Cell, American Society for Cell Biology, 2021, 32 (18), pp.1737-1748. ⟨10.1091/mbc.E21-03-0109⟩. ⟨hal-03366003⟩

Share

Metrics

Record views

20

Files downloads

19