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MBC in Press, published online ahead of print September 7, 2006
Mol. Biol. Cell 10.1091/mbc.E06-04-0260

A more recent version of this article appeared on November 1, 2006 Originally published as MBC in Press, 10.1091/mbc.E06-04-0260 on September 6, 2006
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Submitted on April 3, 2006
Revised on August 14, 2006
Accepted on August 22, 2006

Caenorhabditis elegans DYF-2, an Ortholog of Human WDR19, Is a Component of the IFT Machinery in Sensory Cilia

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

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

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 is poorly understood. Here, we describe a novel WD repeat (WDR) containing IFT protein from C. 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 ortholog of DYF-2, WDR19, also localizes to cilia, pointing to an important evolutionarily conserved role for this WDR protein in cilia development and function.

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




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