Caveolae-associated protein 2 (CAVIN2)

Caveolae-associated protein 2 (CAVIN2), also known as SDPR, is a structural and regulatory protein crucial for the formation and function of caveolae—small invaginations in the plasma membrane involved in signaling, lipid handling, and membrane trafficking[1][3]. CAVIN2 is a phospholipid-binding protein whose expression increases under serum deprivation and is phosphorylated by protein kinase C (PKC)[1]. It acts in concert with caveolin and other cavins, especially in lung and adipose tissue, to regulate caveolae shape, depth of invagination, and integrity[3]. Loss of CAVIN2 leads to decreased caveolae numbers and compromised endothelial function, while its overexpression changes caveolae morphology[1][3]. Functionally, CAVIN2 suppresses inflammatory responses and angiogenesis, particularly through regulation of NF-κB signaling and downstream pro-inflammatory markers like COX-2[5]. It has a documented tumor suppressor role, with gene silencing or methylation in diverse cancers leading to increased cell migration and invasion[3][5]. CAVIN2 interacts with canonical signaling pathways such as ERK1/2, AKT, and STAT3 and may regulate the balance of cell survival versus apoptosis in contexts such as pulmonary injury and metabolic disease[3][5]. There is active investigation into CAVIN2 as a therapeutic target in inflammation, cancer, and cardiovascular disease, although no approved drugs directly target it yet[3][5].

Other names

SDPRSDRPS-p68Serum deprivation-response proteinPhosphatidylserine-binding proteinCavin-2

No FDA-approved drugs specifically targeting Cavin-2; mechanistic studies in inflammation and angiogenesis suggest targeting Cavin-2 may modulate TNF signaling, ERK pathway, caveolae morphology, and downstream pro-inflammatory and proliferative pathways.