Caveolin-1 (CAV1)

Caveolin‑1 is a monotopic integral membrane protein that serves as the principal structural component of caveolae—flask-shaped invaginations found in the plasma membrane of many cell types[3][4][6]. It oligomerizes into disc-shaped complexes embedded within the cytoplasmic leaflet of the lipid bilayer and interacts with cholesterol-rich domains known as lipid rafts[1][5]. Caveolin‑1 acts as a scaffolding molecule, organizing and regulating various signaling molecules including integrins, tyrosine kinases (such as FYN), G proteins, growth factor receptors (EGFR), nitric oxide synthase enzymes, steroid hormone receptors, and others through its conserved scaffolding domain[3]. Functionally, it links integrin subunits to intracellular signaling pathways like Ras–ERK/MAPK to promote cell cycle progression while also acting as a negative regulator in some contexts. The gene encoding this protein is considered a tumor suppressor candidate due to its downregulation or loss in several cancer types. Mutations or altered expression levels have been implicated not only in cancer but also cardiovascular and neurodegenerative diseases. While no approved drugs directly target Caveolin‑1 itself at present, its role at the intersection of multiple signaling pathways makes it an area of ongoing research interest for therapeutic intervention[2][3][8].

Other names

caveolae protein, 22kDaCAV1caveolin 1, caveolae protein, 22kDa (gene/protein product)