Por favor, use este identificador para citar o enlazar este Item:http://hdl.handle.net/20.500.12105/17953
Título
Caveolae - mechanosensitive membrane invaginations linked to actin filaments.
Autor(es)
Echarri, Asier CNIC | Del Pozo, Miguel A
Fecha de publicación
2015-08-01
Cita
J Cell Sci. 2015 Aug 1;128(15):2747-58.
Idioma
Inglés
Tipo de documento
journal article
Resumen
An essential property of the plasma membrane of mammalian cells is its plasticity, which is required for sensing and transmitting of signals, and for accommodating the tensional changes imposed by its environment or its own biomechanics. Caveolae are unique invaginated membrane nanodomains that play a major role in organizing signaling, lipid homeostasis and adaptation to membrane tension. Caveolae are frequently associated with stress fibers, a major regulator of membrane tension and cell shape. In this Commentary, we discuss recent studies that have provided new insights into the function of caveolae and have shown that trafficking and organization of caveolae are tightly regulated by stress-fiber regulators, providing a functional link between caveolae and stress fibers. Furthermore, the tension in the plasma membrane determines the curvature of caveolae because they flatten at high tension and invaginate at low tension, thus providing a tension-buffering system. Caveolae also regulate multiple cellular pathways, including RhoA-driven actomyosin contractility and other mechanosensitive pathways, suggesting that caveolae could couple mechanotransduction pathways to actin-controlled changes in tension through their association with stress fibers. Therefore, we argue here that the association of caveolae with stress fibers could provide an important strategy for cells to deal with mechanical stress.
MESH
Stress, Mechanical | Actomyosin | Animals | Biomechanical Phenomena | Caveolae | Cell Membrane | Humans | Mechanotransduction, Cellular | Protein Structure, Tertiary | Protein Transport | Signal Transduction | Stress Fibers | rhoA GTP-Binding Protein
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