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

Lapierre LA, Ducharme NA, Drake KR, Goldenring JR, Kenworthy AK
Exp Cell Res. 2012 318 (2): 103-13

PMID: 22036648 · PMCID: PMC3230713 · DOI:10.1016/j.yexcr.2011.10.010

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.

MeSH Terms (10)

Animals Caveolin 1 Cell Line Cell Polarity Dogs Endocytosis Endosomes Epithelial Cells Microtubules rab GTP-Binding Proteins

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