Caveolin-1 scaffolding domain (CSD) (CSD)

Caveolin-1 (Cav-1) is a primary structural component of caveolae, which are specialized plasma membrane invaginations involved in vesicular transport and signal transduction (PubMed: 10415088). The Caveolin-1 scaffolding domain (CSD), comprising residues 82-101, acts as a regulatory hub by interacting with Caveolin-binding domains (CBD) or motifs (CBM) on various partner proteins, including eNOS, Src-family kinases, and G-proteins (PubMed: 9312052). This interaction generally serves to sequester these signaling molecules in an inactive state within caveolae. Dysregulation of the CSD-CBD interface is linked to several diseases, including cancer, where Cav-1 can modulate tumor growth and metastasis, and idiopathic pulmonary fibrosis, where CSD-derived peptides show anti-fibrotic activity (PubMed: 22492595). Therapeutic interventions often utilize CSD-mimetic peptides, such as Cavtratin, to competitively inhibit these interactions and restore normal signaling, particularly in inflammatory and vascular disorders (PubMed: 11114892).

Other names

Caveolin-1 scaffolding domain / caveolin-binding domain interfaceCSD-CBD interactionCaveolin-binding motifCBMCav-1 scaffolding domain

Competitive inhibition of the interaction between the Caveolin-1 scaffolding domain and partner proteins containing Caveolin-binding motifs (CBM), thereby modulating the activity of signaling enzymes like eNOS and Src (PubMed: 9312052).