Abstract

Although they were discovered more than 50 years ago, caveolae have remained enigmatic plasmalemmal organelles. With their characteristic “flasklike” shape and virtually ubiquitous tissue distribution, these interesting structures have been implicated in a wide range of cellular functions. Similar to clathrin-coated pits, caveolae function as macromolecular vesicular transporters, while their unique lipid composition classifies them as plasma membrane lipid rafts, structures enriched in a variety of signaling molecules. The caveolin proteins (caveolin-1, -2, and -3) serve as the structural components of caveolae, while also functioning as scaffolding proteins, capable of recruiting numerous signaling molecules to caveolae, as well as regulating their activity. That so many signaling molecules and signaling cascades are regulated by an interaction with the caveolins provides a paradigm by which numerous disease processes may be affected by ablation or mutation of these proteins. Indeed, studies in caveolin-deficient mice have implicated these structures in a host of human diseases, including diabetes, cancer, cardiovascular disease, atherosclerosis, pulmonary fibrosis, and a variety of degenerative muscular dystrophies. In this review, we provide an in depth summary regarding the mechanisms by which caveolae and caveolins participate in human disease processes.

Keywords

CaveolaeDiseaseCaveolin 3Cell biologyBiologyChemistryMedicineInternal medicineSignal transduction

MeSH Terms

Amino Acid SequenceAnimalsCaveolaeCaveolin 1CaveolinsDiseaseHumansMolecular Sequence DataSequence HomologySignal Transduction

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Publication Info

Year
2004
Type
review
Volume
84
Issue
4
Pages
1341-1379
Citations
898
Access
Closed

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898
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43
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702
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Cite This

Alex W. Cohen, Robert Hnasko, William Schubert et al. (2004). Role of Caveolae and Caveolins in Health and Disease. Physiological Reviews , 84 (4) , 1341-1379. https://doi.org/10.1152/physrev.00046.2003

Identifiers

DOI
10.1152/physrev.00046.2003
PMID
15383654

Data Quality

Data completeness: 81%