Caveolae are designated as specialized small plasma-membrane subdomains that play critical cellular functions through the regulation of trafficking and signal transductions. It is proved that two essential protein families, membrane caveolins, and cytoplasmic cavin proteins, are required for the caveola formation. Caveolins are present in the majority of adherent, mammalian cells. There are three members for caveolin gene family in vertebrates, including CAV1, CAV2, and CAV3, encoding corresponding proteins caveolin-1, caveolin-2, and caveolin-3, respectively. All these members are membrane proteins with similar in structure, involving an N-terminal caveolin scaffolding domain (CSD), a transmembrane domain as well as a C-terminal domain. The CSD and C-terminal are sufficient for the caveolin attachment to cell membranes, even without a membrane-spanning domain. Caveolins form oligomers and correlate with cholesterol and sphingolipids in certain membrane areas, leading to the constitution of caveolae. Furthermore, caveolin has a paradoxical role in the development of oncogenesis. This protein is involved in cancer formation and suppression, which depends on the tumor type and progress stage.
The caveolin family consists of three type proteins, CAV1-3, and here shows part of caveolins. There exist two isoforms for CAV1, caveolin-1α and caveolin-1β, the latter lacking a part of the N-terminus. CAV1 is indispensable for the caveolae formation while CAV2 is not, whose expression and membrane localization rely on CAV1. CAV3 as a muscle-specific isoform is also required for the caveolae formation in cardiac and skeletal muscle cells.
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