Description
The CAV1 gene encodes caveolin-1, an integral membrane protein abundant in the endothelium and other cells in the lung. It is the main component of the flask-like invaginations of the plasma membrane known as caveolae (summary by Austin et al., 2012).
Cloning and Expression
Glenney (1992) cloned and sequenced a human cDNA encoding caveolin from lung. He observed a striking sequence similarity to the vesicle transport protein VIP21 (see Kurzchalia et al., 1992). Scherer et al. (1996) reviewed the literature on caveolin. Structurally, caveolin can be divided into 3 distinct regions: a hydrophilic cytosolic N-terminal domain, a membrane-spanning region, and a hydrophilic C-terminal domain. The C-terminal domain undergoes palmitoylation (S-acylation) on 3 cysteine residues, suggesting that both the membrane-spanning region and the C-terminal domain of caveolin are associated with the membrane. They stated that caveolin may function as a scaffolding protein for organizing and concentrating certain caveolin-interacting molecules within caveolae membranes.
The CAV1 gene is translated as a full-length protein of 178 amino acids in its alpha isoform. Using immunohistochemical studies, Austin et al. (2012) found that CAV1 is expressed primarily on the endothelial cell surface of pulmonary arteries, with some staining in the cytoplasm of endothelial cells.
The CAV1 gene encodes caveolin-1, an integral membrane protein abundant in the endothelium and other cells in the lung. It is the main component of the flask-like invaginations of the plasma membrane known as caveolae (summary by Austin et al., 2012).
Cloning and Expression
Glenney (1992) cloned and sequenced a human cDNA encoding caveolin from lung. He observed a striking sequence similarity to the vesicle transport protein VIP21 (see Kurzchalia et al., 1992). Scherer et al. (1996) reviewed the literature on caveolin. Structurally, caveolin can be divided into 3 distinct regions: a hydrophilic cytosolic N-terminal domain, a membrane-spanning region, and a hydrophilic C-terminal domain. The C-terminal domain undergoes palmitoylation (S-acylation) on 3 cysteine residues, suggesting that both the membrane-spanning region and the C-terminal domain of caveolin are associated with the membrane. They stated that caveolin may function as a scaffolding protein for organizing and concentrating certain caveolin-interacting molecules within caveolae membranes.
The CAV1 gene is translated as a full-length protein of 178 amino acids in its alpha isoform. Using immunohistochemical studies, Austin et al. (2012) found that CAV1 is expressed primarily on the endothelial cell surface of pulmonary arteries, with some staining in the cytoplasm of endothelial cells.