Mechano-sensing at the cell membrane may involves change of conformation of proteins under stress, such as the opening of mechanically-gated channels or the unfolding adhesion proteins. Another class of mechano-sensing systems involves the assembly and disassembly of multi-protein complexes. In this talk, I will discuss the case of caveoale, small invaginated nanodomains at the plasma membrane of many cell types that have been classically involved in membrane trafficking and signaling. After presenting experimental evidence - obtained by collaborators - of the role of caveolae mechanics in the control of different signaling pathway, I will describe a thermodynamic model of caveolae stability under tension based on the phase separation of membrane-associated proteins into invaginated, multi-component membrane domains. I will in particular discuss the importance of the multi-component nature of caveolae, enriched in the curvature-generating membrane protein caveolin, and stabilised by the curvature-dependent binding of cytosolic proteins, including cavin which can form a rigid coat over the caveolin domains, and the ATPase EHD2 which can form ring-like oligomers at the caveolae neck.

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