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Caenorhabditis eleg...
Caenorhabditis elegans DYF-2, an orthologue of human WDR19, is a component of the intraflagellar transport machinery in sensory Cilia
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- Efimenko, Evgeni (författare)
- Södertörns högskola,Institutionen för livsvetenskaper,Karolinska Institute
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- Blacque, Oliver E. (författare)
- Simon Fraser University, Burnaby, British Columbia, Canada
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- Ou, Guangshuo (författare)
- University of California, Davis, USA
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- Haycraft, Courtney J. (författare)
- University of Alabama at Birmingham Medical Center, Birmingham, USA
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- Yoder, Bradley K. (författare)
- University of Alabama at Birmingham Medical Center, Birmingham, USA
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- Scholey, Jonathan M. (författare)
- University of California, Davis, USA
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- Leroux, Michel R. (författare)
- Simon Fraser University, Burnaby, British Columbia, Canada
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- Swoboda, Peter (författare)
- Karolinska Institutet,Södertörns högskola,Institutionen för livsvetenskaper,Karolinska Instiute
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(creator_code:org_t)
- 2006
- 2006
- Engelska.
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Ingår i: Molecular Biology of the Cell. - 1059-1524 .- 1939-4586. ; 17:11, s. 4801-4811
- Relaterad länk:
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https://doi.org/10.1...
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http://www.ncbi.nlm....
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https://urn.kb.se/re...
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https://doi.org/10.1...
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http://kipublication...
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Abstract
Ämnesord
Stäng
- 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.
Ämnesord
- NATURVETENSKAP -- Biologi -- Cellbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Cell Biology (hsv//eng)
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