Caveolae formation has raised the concept of energy efficiency to new heights. The ultimate purpose of caveolae formation is to colocalize signaling proteins with membrane microdomains in order to facilitate their interaction and improve signal transduction efficiency. Although we know that the main structural protein of caveolae is caveolin, how caveolin interacts with membrane proteins to facilitate their integration into lipid raft domains is unclear. A caveolin-scaffolding domain (CSD) on caveolin itself can associate with membrane proteins such as G proteins and endothelial nitric oxide synthase. In this issue, Kwiatek et al. (p. 1174) report that the TRPC1 channel protein contains a C-terminal CSD-consensus binding sequence that allows for its physical and functional interaction with caveolin-1 in the caveolae of human pulmonary artery endothelial cells (PAEC). Competitive interaction with a CSD-conjugated peptide attenuates thrombin- and thapsigargin-induced Ca2+ influx via store-operated TRPC1 channels. Their data suggest that caveolin-1 can directly regulate TRPC1 function, extending its already ascribed role as a structural protein.