2026-04-27T01:59:19Zhttps://repisalud.isciii.es/rest/oai/requestoai:repisalud.isciii.es:20.500.12105/89362024-10-31T11:44:34Zcom_20.500.12105_19604com_20.500.12105_2051col_20.500.12105_19605col_20.500.12105_19607
Repisalud
author
Echarri, Asier
author
Pavon, Dacil Maria
author
Sanchez, Sara
author
Garcia-Garcia, Maria
author
Calvo, Enrique
author
Huerta-Lopez, Carla
author
Velazquez-Carreras, Diana
author
Viaris de Lesegno, Christine
author
Ariotti, Nicholas
author
Lázaro-Carrillo, Ana
author
Strippoli, Raffaele
author
De Sancho, David
author
Alegre-Cebollada, Jorge
author
Lamaze, Christophe
author
Parton, Robert G
author
del Pozo, Miguel Angel
funder
Ministerio de Economía, Industria y Competitividad (España)
funder
European Regional Development Fund
funder
Fundación La Marató TV3
funder
Worldwide Cancer Research
funder
Unión Europea. Comisión Europea
funder
Ministerio de Ciencia, Innovación y Universidades (España)
funder
Comunidad de Madrid (España)
funder
Agence Nationale de la Recherche (Francia)
funder
Fondation ARC pour la recherche sur le cancer
funder
National Health and Medical Research Council (Australia)
funder
Instituto de Salud Carlos III
funder
Fundación ProCNIC
2020-01-29T11:29:08Z
2020-01-29T11:29:08Z
2019-12-20
Nat Commun. 2019; 10(1):5828
2041-1723
http://hdl.handle.net/20.500.12105/8936
31862885
10.1038/s41467-019-13782-2
2041-1723
Nature communications
Cells remodel their structure in response to mechanical strain. However, how mechanical forces are translated into biochemical signals that coordinate the structural changes observed at the plasma membrane (PM) and the underlying cytoskeleton during mechanoadaptation is unclear. Here, we show that PM mechanoadaptation is controlled by a tension-sensing pathway composed of c-Abl tyrosine kinase and membrane curvature regulator FBP17. FBP17 is recruited to caveolae to induce the formation of caveolar rosettes. FBP17 deficient cells have reduced rosette density, lack PM tension buffering capacity under osmotic shock, and cannot adapt to mechanical strain. Mechanistically, tension is transduced to the FBP17 F-BAR domain by direct phosphorylation mediated by c-Abl, a mechanosensitive molecule. This modification inhibits FBP17 membrane bending activity and releases FBP17-controlled inhibition of mDia1-dependent stress fibers, favoring membrane adaptation to increased tension. This mechanoprotective mechanism adapts the cell to changes in mechanical tension by coupling PM and actin cytoskeleton remodeling.
eng
An Abl-FBP17 mechanosensing system couples local plasma membrane curvature and stress fiber remodeling during mechanoadaptation
journal article
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