Caveolae are plasma membrane invaginations involved in multiple intracellular processes such as endocytosis, cell migration, vesicular transport and membrane tension sensing. Caveolae are known to protect cells under mechanical stress by providing an extra membrane reservoir through caveolar flattening thus relieving mechanical tension at the plasma membrane. Their formation depends upon multiple interactions between membrane-embedded caveolins, lipids and cytosolic cavin proteins. Of the four cavin family members, only cavin1 is strictly required for caveola formation. The cavin proteins have a distinctive domain architecture possessing N- and C-terminal helical regions alternating with three disordered domains (DR1, DR2, DR3). A minimal N-terminal domain of the cavins, termed helical region 1 (HR1) is required and sufficient for cavin proteins homo- and hetero-oligomerization. Crystal structures of the mouse cavin1 and zebrafish cavin4a HR1 domains reveal highly conserved extended trimeric coiled-coil architectures, with inter subunit interactions that determine the specificity of cavin-cavin interactions (1). The C-terminal helical region contains an eleven residue repeat sequence exclusive to cavin1 (Undecad of cavin1 – UC1 domain) that is essential for its localisation to caveolae (2). The HR1 and UC1 domains possess a basic surface exposed patch of amino acids that interacts with specific membrane lipids such as poly-phosphoinositides and phosphatidylserine. The UC1 domain of cavin1 plays a crucial role in modulating the caveolar disassembly response in cells under mechanical stress (2). The HR1 and UC1 domains of cavin1 co-ordinate with the disordered domains to form large oligomers via a novel mechanism that promote membrane remodelling. Overall cavins possess an extensive membrane sculpting activity that results in a formation of membrane tubules in vitro. Lastly, we reveal that the rod like coiled-coil domain architecture of cavins form a filamentous coat on the surface of caveolae.