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MBC in Press, published online ahead of print April 26, 2006
Mol. Biol. Cell 10.1091/mbc.E05-08-0799

A more recent version of this article appeared on July 1, 2006
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Submitted on August 25, 2005
Revised on March 21, 2006
Accepted on April 14, 2006

Rab10 Regulates Membrane Transport through Early Endosomes of Polarized Madin-Darby Canine Kidney Cells

Clifford M. Babbey,* Nahid Ahktar,* Exing Wang,* Carlos Chih-Hsiung Chen,{dagger} Barth Grant,{dagger} and Kenneth W. Dunn*

*Department of Medicine, Division of Nephrology, Indiana University Medical Center, Indianapolis, IN 46202; {dagger}Department of Molecular Biology and Biochemistry, Rutgers University, Piscataway, NJ 08854

Monitoring Editor: Keith Mostov

Rab10, a protein originally isolated from Madin-Darby Canine Kidney (MDCK) epithelial cells, belongs to a family of Rab proteins that includes Rab8 and Rab13. While both Rab8 and Rab13 have been found to mediate polarized membrane transport, the function of Rab10 in mammalian cells has not yet been established. We have used quantitative confocal microscopy of polarized MDCK cells expressing GFP chimeras of wild-type and mutant forms of Rab10 to analyze the function of Rab10 in polarized cells. These studies demonstrate that Rab10 is specifically associated with the common endosomes of MDCK cells, accessible to endocytic probes internalized from either the apical or basolateral plasma membrane domains. Expression of mutant Rab10 defective for either GTP hydrolysis or GTP binding increased recycling from early compartments on the basolateral endocytic pathway without affecting recycling from later compartments or the apical recycling pathway. These results suggest that Rab10 mediates transport from basolateral sorting endosomes to common endosomes.

Address correspondence to: Kenneth W. Dunn (kwdunn{at}iupui.edu)




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