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Vol. 16, Issue 4, 2091-2105, April 2005
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* Institute for Molecular Bioscience, Centre for Microscopy and Microanalysis and School of Biomedical Sciences, University of Queensland, Queensland 4072, Australia;
Departament de Biologia Cellular, Facultat de Medicina, Institut d'Investigacions Biomèdiques August Pi Sunyer, Universitat de Barcelona, 08036 Barcelona, Spain
Submitted August 25, 2004;
Revised January 18, 2005;
Accepted January 21, 2005
Monitoring Editor: Benjamin Glick
Caveolins are a crucial component of plasma membrane (PM) caveolae but have also been localized to intracellular compartments, including the Golgi complex and lipid bodies. Mutant caveolins associated with human disease show aberrant trafficking to the PM and Golgi accumulation. We now show that the Golgi pool of mainly newly synthesized protein is detergent-soluble and predominantly in a monomeric state, in contrast to the surface pool. Caveolin at the PM is not recognized by specific caveolin antibodies unless PM cholesterol is depleted. Exit from the Golgi complex of wild-type caveolin-1 or -3, but not vesicular stomatitis virus-G protein, is modulated by changing cellular cholesterol levels. In contrast, a muscular dystrophy-associated mutant of caveolin-3, Cav3P104L, showed increased accumulation in the Golgi complex upon cholesterol treatment. In addition, we demonstrate that in response to fatty acid treatment caveolin can follow a previously undescribed pathway from the PM to lipid bodies and can move from lipid bodies to the PM in response to removal of fatty acids. The results suggest that cholesterol is a rate-limiting component for caveolin trafficking. Changes in caveolin flux through the exocytic pathway can therefore be an indicator of cellular cholesterol and fatty acid levels.
Abbreviations used: BHK, baby hamster kidney; CavDGV, caveolin 3 DGV truncation; CD, cyclodextrin; Cyhx, cycloheximide; ER, endoplasmic reticulum; FRAP, fluorescence recovery after photobleaching; GFP, green fluorescent protein; HA, hemagglutinin; LB, lipid body; PM, plasma membrane; TGN, trans-Golgi network; TX-100, Triton X-100; VSV-G, vesicular stomatitis virus-G protein.
The online version of this article contains supplemental material at MBC Online (http://www.molbiolcell.org).
Address correspondence to: Robert G. Parton (r.parton{at}imb.uq.edu.au) or Albert Pol (apols{at}ub.edu).
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