Caveolin-1 (CAV1) (CAV1)

Caveolin-1 (CAV1) is the essential structural protein required for the formation of caveolae, which are 50-100 nm flask-shaped invaginations of the plasma membrane [UniProt: P33176, Nat Rev Mol Cell Biol. 2007; 8(3): 185-194]. These structures, often associated with lipid rafts, serve as specialized platforms for signal transduction, endocytosis, and mechanotransduction. Caveolin-1 functions primarily as a scaffolding protein, interacting with and regulating the activity of various signaling molecules such as Src-family kinases, H-Ras, and endothelial nitric oxide synthase (eNOS) through its highly conserved scaffolding domain [NCBI Gene: 857]. In oncology, Caveolin-1 exhibits a complex, context-dependent role, acting as a tumor suppressor in early stages but frequently promoting migration, invasion, and multi-drug resistance in advanced metastatic cancers [J Exp Clin Cancer Res. 2016; 35: 190]. Beyond cancer, it is critically implicated in the pathogenesis of pulmonary fibrosis, atherosclerosis, and metabolic disorders due to its role in lipid homeostasis and vascular signaling. Therapeutic strategies targeting Caveolin-1 include the use of mimetic peptides to restore its scaffolding function or small molecules that disrupt caveolae to enhance drug delivery or inhibit pathological signaling.

Other names

VIP21P144Caveolae protein 1Cell growth-inhibiting protein 32

Modulation of signaling pathways through the Caveolin Scaffolding Domain (CSD) and regulation of caveolae-mediated endocytosis and membrane trafficking [UniProt: P33176, Nat Rev Mol Cell Biol. 2007; 8(3): 185-194].