The amino acid sequence of caveolin-1 predicts that it is an integral membrane protein, and
there is strong experimental evidence that it has this property. For example, caveolin-1 is
cotranslationally inserted into the ER1 and shipped to the Golgi apparatus where it is
incorporated into lipid domains that sort molecules for shipment to the cell surface (1). The
preferred location for caveolin-1 at the cell surface is the caveola, and it cannot be removed
from these membranes without detergent (2). Finally, the movements of green fluorescent …