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Exp Cell Res. 2012 Jan 15;318(2):103-13. doi: 10.1016/j.yexcr.2011.10.010. Epub 2011 Oct 20.

Coordinated regulation of caveolin-1 and Rab11a in apical recycling compartments of polarized epithelial cells.

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  • 1Department of Surgery, Vanderbilt University School of Medicine, Nashville, TN 37232-0443, USA.


Recent studies have identified caveolin-1, a protein best known for its functions in caveolae, in apical endocytic recycling compartments in polarized epithelial cells. However, very little is known about the regulation of caveolin-1 in the endocytic recycling pathway. To address this question, in the current study we compared the relationship between compartments enriched in sub-apical caveolin-1 and Rab11a, a well-defined marker of apical recycling endosomes, using polarized MDCK cells as a model. We show that caveolin-1-containing vesicles define a compartment that partially overlaps with Rab11a, and that the distribution of subapical caveolin-1 and Rab11a shows a similar dependence on microtubule disruption. Mutants of the Rab11a effector, Rab11-FIP2 also altered the localization of caveolin-1. These findings indicate that caveolin-1 is coordinately regulated with Rab11a within the apical recycling system of polarized epithelial cells, suggesting that the two proteins are components of the same pathway.

Copyright © 2011 Elsevier Inc. All rights reserved.

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