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MBC in Press, published online ahead of print January 19, 2005
Mol. Biol. Cell 10.1091/mbc.E04-08-0760

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Submitted on August 31, 2004
Accepted on January 11, 2005

Regulation of Membrane Trafficking by a Novel Cdc42-related Protein in Caenorhabditis elegans Epithelial Cells

S. Jenna,*{dagger}{ddagger} M.-E. Caruso,* A. Emadali,* D. T. Nguyên,* M. Dominguez,{sect} S. Li,|| R. Roy,|| J. Reboul,¶# M. Vidal,¶ G. N. Tzimas,* R. Bossé,** and E. Chevet*{dagger}{ddagger}

*Organelle Signaling Laboratory, Department of Surgery and {dagger}Montreal Proteomics Network, McGill University, Montreal, Quebec, Canada H3A 1A1; {sect}HyperOmics Farma Inc., Montreal, Quebec, Canada H9H 4K8; ||Biology Department, McGill University, Montreal, Quebec, Canada H3A 1B1; Center for Cancer Systems Biology and Department of Cancer Biology, Dana-Farber Cancer Institute, and Department of Genetics, Harvard Medical School, Boston, MA 02115; **Perkin-Elmer-Biosignal, Montreal, Quebec, Canada H3J 1R4

Monitoring Editor: Martin A. Schwartz

Rho GTPases are mainly known for their implication in cytoskeleton remodeling. They have also been recently shown to regulate various aspects of membrane trafficking. Here, we report the identification and the characterization of a novel Caenorhabditis elegans Cdc42-related protein, CRP-1, that shows atypical enzymatic characteristics in vitro. Expression in mouse fibroblasts revealed that, in contrast with CDC-42, CRP-1 was unable to reorganize the actin cytoskeleton and mainly localized to trans-Golgi network and recycling endosomes. This subcellular localization, as well as its expression profile restricted to a subset of epithelial-like cells in C. elegans, suggested a potential function for this protein in polarized membrane trafficking. Consistent with this hypothesis, alteration of CRP-1 expression affected the apical trafficking of CHE-14 in vulval and rectal epithelial cells and sphingolipids (C6-NBD-ceramide) uptake and/or trafficking in intestinal cells. However, it did not affect basolateral trafficking of Myotactin in the pharynx and the targeting of IFB-2 and AJM-1, two cytosolic apical markers of intestine epithelial cells. Hence, our data demonstrate a function for CRP-1 in the regulation of membrane trafficking in a subset of cells with epithelial characteristics.

#Present address: INSERM, Unité 119, Institut Paoli Calmettes, 13009 Marseille, France.

{ddagger}Corresponding authors. E-mail: sarah.jenna{at}mcgill.ca E-mail: eric.chevet{at}mcgill.ca




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