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MBC in Press, published online ahead of print January 10, 2006
Mol. Biol. Cell 10.1091/mbc.E05-08-0787

A more recent version of this article appeared on March 1, 2006 Originally published as MBC in Press, 10.1091/mbc.E05-08-0787 on January 4, 2006
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Submitted on August 22, 2005
Revised on December 27, 2005
Accepted on December 28, 2005

RAB-10 Is Required for Endocytic Recycling in the C. elegans Intestine

Carlos Chih-Hsiung Chen,* Peter J. Schweinsberg,* Shilpa Vashist,* Darren P. Mareiniss,{dagger} Eric J. Lambie,{dagger} and Barth D. Grant*

*Department of Molecular Biology and Biochemistry, Rutgers University, Piscataway, NJ 08854; {dagger}Department of Biological Sciences, Dartmouth College, Hanover, NH 03755

Monitoring Editor: Keith Mostov

The endocytic pathway of eukaryotes is essential for the internalization and trafficking of macromolecules, fluid, membranes, and membrane proteins. One of the most enigmatic aspects of this process is endocytic recycling, the return of macromolecules (often receptors) and fluid from endosomes to the plasma membrane. We have previously shown that the EH-domain protein RME-1 is a critical regulator of endocytic recycling in worms and mammals. Here we identify the RAB-10 protein as a key regulator of endocytic recycling upstream of RME-1 in polarized epithelial cells of the C. elegans intestine. rab-10 null mutant intestinal cells accumulate abnormally abundant RAB-5 positive early endosomes, some of which are enlarged by more than 10-fold. Conversely most RME-1 positive recycling endosomes are lost in rab-10 mutants. The abnormal early endosomes in rab-10 mutants accumulate basolaterally recycling transmembrane cargo molecules, and basolaterally recycling fluid, consistent with a block in basolateral transport. These results indicate a role for RAB-10 in basolateral recycling upstream of RME-1. We found that a functional GFP-RAB-10 reporter protein is localized to endosomes and Golgi in wild-type intestinal cells consistent with a direct role for RAB-10 in this transport pathway.

Address correspondence to: Barth D. Grant (grant{at}biology.rutgers.edu)




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