Complementary mesoscale dynamics of spectrin and acto-myosin shape membrane territories during mechanoresponse

Andrea Ghisleni (), Camilla Galli, Pascale Monzo, Flora Ascione, Marc-Antoine Fardin, Giorgio Scita, Qingsen Li, Paolo Maiuri and Nils C. Gauthier ()
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Andrea Ghisleni: Institute FIRC of Molecular Oncology (IFOM)
Camilla Galli: Institute FIRC of Molecular Oncology (IFOM)
Pascale Monzo: Institute FIRC of Molecular Oncology (IFOM)
Flora Ascione: Institute FIRC of Molecular Oncology (IFOM)
Marc-Antoine Fardin: Institut Jacques Monod, Centre National de la Recherche Scientifique UMR 7592 and Université Paris Diderot
Giorgio Scita: Institute FIRC of Molecular Oncology (IFOM)
Qingsen Li: Institute FIRC of Molecular Oncology (IFOM)
Paolo Maiuri: Institute FIRC of Molecular Oncology (IFOM)
Nils C. Gauthier: Institute FIRC of Molecular Oncology (IFOM)

Nature Communications, 2020, vol. 11, issue 1, 1-21

Abstract: Abstract The spectrin-based membrane skeleton is a major component of the cell cortex. While expressed by all metazoans, its dynamic interactions with the other cortex components, including the plasma membrane or the acto-myosin cytoskeleton, are poorly understood. Here, we investigate how spectrin re-organizes spatially and dynamically under the membrane during changes in cell mechanics. We find spectrin and acto-myosin to be spatially distinct but cooperating during mechanical challenges, such as cell adhesion and contraction, or compression, stretch and osmolarity fluctuations, creating a cohesive cortex supporting the plasma membrane. Actin territories control protrusions and contractile structures while spectrin territories concentrate in retractile zones and low-actin density/inter-contractile regions, acting as a fence that organize membrane trafficking events. We unveil here the existence of a dynamic interplay between acto-myosin and spectrin necessary to support a mesoscale organization of the lipid bilayer into spatially-confined cortical territories during cell mechanoresponse.

Date: 2020
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DOI: 10.1038/s41467-020-18825-7

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