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Originally published as MBoC in Press, 10.1091/mbc.E08-08-0837 on January 21, 2009

Vol. 20, Issue 6, 1763-1771, March 15, 2009

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Caveolin-2 Is Required for Apical Lipid Trafficking and Suppresses Basolateral Recycling Defects in the Intestine of Caenorhabditis elegans

Scott Parker*,{dagger}, Denise S. Walker{dagger},{ddagger}, Sung Ly, and Howard A. Baylis

Department of Zoology, University of Cambridge, Downing Street, Cambridge, CB2 3EJ, United Kingdom

Submitted August 14, 2008; Revised December 8, 2008; Accepted January 13, 2009
Monitoring Editor: Jennifer Lippincott-Schwartz

Caveolins are plasma membrane–associated proteins that colocalize with, and stabilize caveolae. Their functions remain unclear although they are known to be involved in specific events in cell signaling and endocytosis. Caenorhabditis elegans encodes two caveolin genes, cav-1 and cav-2. We show that cav-2 is expressed in the intestine where it is localized to the apical membrane and in intracellular bodies. Using the styryl dye FM4-64 and BODIPY-labeled lactosylceramide, we show that the intestinal cells of cav-2 animals are defective in the apical uptake of lipid markers. These results suggest parallels with the function of caveolins in lipid homeostasis in mammals. We also show that CAV-2 depletion suppresses the abnormal accumulation of vacuoles that result from defective basolateral recycling in rme-1 and rab-10 mutants. Analysis of fluorescent markers of basolateral endocytosis and recycling suggest that endocytosis is normal in cav-2 mutants and thus, that the suppression of basolateral recycling defects in cav-2 mutants is due to changes in intracellular trafficking pathways. Finally, cav-2 mutants also have abnormal trafficking of yolk proteins. Taken together, these data indicate that caveolin-2 is an integral component of the trafficking network in the intestinal cells of C. elegans.

This article was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E08-08-0837) on January 21, 2009.

{dagger} These authors contributed equally to this work.

Present addresses: *Saint Louis University Medical School, St. Louis, MO 63104;

{ddagger}MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, United Kingdom.

Address correspondence to: Howard A. Baylis (hab{at}mole.bio.cam.ac.uk)




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