Role of plasmalemmal caveolae in signal transduction

• Published in: American journal of physiology. Lung cellular and molecular physiology Vol. 275; no. 5; pp. 843 - L851
• Main Authors: Shaul, Philip W, Anderson, Richard G. W
• Format: Journal Article
• Language: English
• Published: United States 01.11.1998
• Subjects: Animals; Cell Membrane - physiology; Cell Membrane - ultrastructure; GTP-Binding Proteins - metabolism; Humans; Membrane Lipids - physiology; Phospholipids - physiology; Receptors, Cell Surface - physiology; Signal Transduction - physiology
• ISSN: 1040-0605; 0002-9513; 1522-1504
• DOI: 10.1152/ajplung.1998.275.5.l843

Departments of 1  Pediatrics and 2  Cell Biology and Neuroscience, University of Texas Southwestern Medical Center at Dallas, Dallas, Texas 75235-9063 Caveolae are specialized plasmalemmal microdomains originally studied in numerous cell types for their involvement in the transcytosis of macromolecules. They are enriched in glycosphingolipids, cholesterol, sphingomyelin, and lipid-anchored membrane proteins, and they are characterized by a light buoyant density and resistance to solubilization by Triton X-100 at 4°C. Once the identification of the marker protein caveolin made it possible to purify this specialized membrane domain, it was discovered that caveolae also contain a variety of signal transduction molecules. This includes G protein-coupled receptors, G proteins and adenylyl cyclase, molecules involved in the regulation of intracellular calcium homeostasis, and their effectors including the endothelial isoform of nitric oxide synthase, multiple components of the tyrosine kinase-mitogen-activated protein kinase pathway, and numerous lipid signaling molecules. More recent work has indicated that caveolae further serve to compartmentalize, modulate, and integrate signaling events at the cell surface. This specialized plasmalemmal domain warrants direct consideration in future investigations of both normal and pathological signal transduction in pulmonary cell types. adenylyl cyclase; caveolin; cholesterol; endothelial nitric oxide synthase; mitogen-activated protein kinase