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Vol. 17, Issue 11, 4801-4811, November 2006

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Caenorhabditis elegans DYF-2, an Orthologue of Human WDR19, Is a Component of the Intraflagellar Transport Machinery in Sensory Cilia

Evgeni Efimenko^*, Oliver E. Blacque, Guangshuo Ou, Courtney J. Haycraft, Bradley K. Yoder, Jonathan M. Scholey, Michel R. Leroux, and Peter Swoboda^*

*Karolinska Institute, Department of Biosciences and Nutrition, Södertörn University College, School of Life Sciences, S-14189 Huddinge, Sweden; Department of Molecular Biology and Biochemistry, Simon Fraser University, Burnaby, British Columbia, V5A 1S6 Canada; Center for Genetics and Development, Section of Molecular and Cellular Biology, University of California, Davis, Davis, CA 95616; and Department of Cell Biology, University of Alabama at Birmingham Medical Center, Birmingham, AL 35294

Submitted April 3, 2006; Revised August 14, 2006; Accepted August 22, 2006
Monitoring Editor: Erika Holzbaur

The intraflagellar transport (IFT) machinery required to build functional cilia consists of a multisubunit complex whose molecular composition, organization, and function are poorly understood. Here, we describe a novel tryptophan-aspartic acid (WD) repeat (WDR) containing IFT protein from Caenorhabditis elegans, DYF-2, that plays a critical role in maintaining the structural and functional integrity of the IFT machinery. We determined the identity of the dyf-2 gene by transgenic rescue of mutant phenotypes and by sequencing of mutant alleles. Loss of DYF-2 function selectively affects the assembly and motility of different IFT components and leads to defects in cilia structure and chemosensation in the nematode. Based on these observations, and the analysis of DYF-2 movement in a Bardet–Biedl syndrome mutant with partially disrupted IFT particles, we conclude that DYF-2 can associate with IFT particle complex B. At the same time, mutations in dyf-2 can interfere with the function of complex A components, suggesting an important role of this protein in the assembly of the IFT particle as a whole. Importantly, the mouse orthologue of DYF-2, WDR19, also localizes to cilia, pointing to an important evolutionarily conserved role for this WDR protein in cilia development and function.

This article was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E06-04-0260) on September 7, 2006.

Address correspondence to: Peter Swoboda (peter.swoboda{at}biosci.ki.se)

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