Short name: CAV-1
Overlapping homologous superfamilies
- Caveolin (IPR001612)
- Caveolin-1 (IPR015504)
Caveolin-1 (CAV-1) is a structural components of caveolae, which are 50-100 nm invaginations of the plasma membrane that play various physiological roles. CAV1 associates with cavin-1 and is confined to the plasma membrane [PMID: 26725982]. CAV-1 has several functions, for instance, it regulates TCR signal strength and regulatory T cell differentiation into alloreactive T cells [PMID: 26837700]. It can also affect the permeability of blood-tumour barrier (BTB) by regulating the expression of tight junction-associated proteins [PMID: 26722502].
Caveolae are 50-100 nm invaginations located at the plasma membrane of many cell types and are known to transport molecules across endothelial cells [PMID: 9759488]. Caveolae require the caveolin protein for formation. Caveolins may act as scaffolding proteins within caveolar membranes by compartmentalizing and concentrating signalling molecules. Mammals have three caveolin proteins:caveolin-1 (Cav-1, or VIP21), caveolin-2 and caveolin-3 (or M-caveolin). Various classes of signalling molecules, including G-protein subunits, receptor and non-receptor tyrosine kinases, endothelial nitric oxide synthase (eNOS), and small GTPases, bind Cav-1 through its 'caveolin-scaffolding domain' [PMID: 23028656].
Caveolins are proteins of about 20 Kd, they form high molecular mass homo-oligomers. Structurally they seem to have N-terminal and C-terminal hydrophilic segments and a long central transmembrane domain that probably forms a hairpin in the membrane. Both extremities are known to face the cytoplasm. Caveolae are enriched with cholesterol and Cav-1 is one of the few proteins that binds cholesterol tightly and specifically.
- PTHR10844:SF18 (PTHR10844:SF18)