Caveolae (also known as plasmalemmal vesicles) are 50-100 nM flask-shaped membranes that represent a subcompartment of the plasma membrane. On the basis of morphological studies, caveolae have been implicated to function in the transcytosis of various macromolecules (including LDL) across capillary endothelial cells, uptake of small molecules via potocytosis and the compartmentalization of certain signaling molecules including G protein-coupled receptors. Three proteins, caveolin-1, caveolin-2 and caveolin-3, have been identified as principal components of caveolae. Two forms of caveolin-1, designated alpha and beta, share a distinct but overlapping cellular distribution and differ by an amino terminal 31 amino acid sequence which is absent from the beta isoform. Caveolin-1 shares 31% identity with caveolin-2 and 65% identity with caveolin-3 at the amino acid level. Functionally, the three proteins differ in their interactions with heterotrimeric G protein isoforms.