|ZFIN ID: ZDB-PUB-100614-31|
Chlamydomonas IFT70/CrDYF-1 Is a Core Component of IFT Particle Complex B and Is Required for Flagellar Assembly
Fan, Z.C., Behal, R.H., Geimer, S., Wang, Z., Williamson, S.M., Zhang, H., Cole, D.G., and Qin, H.
|Source:||Molecular biology of the cell 21(15): 2696-2706 (Journal)|
|PubMed:||20534810 Full text @ Mol. Biol. Cell|
Fan, Z.C., Behal, R.H., Geimer, S., Wang, Z., Williamson, S.M., Zhang, H., Cole, D.G., and Qin, H. (2010) Chlamydomonas IFT70/CrDYF-1 Is a Core Component of IFT Particle Complex B and Is Required for Flagellar Assembly. Molecular biology of the cell. 21(15):2696-2706.
ABSTRACTMonitoring Editor: Tim Stearns DYF-1 is a highly conserved protein essential for ciliogenesis in several model organisms. In Caenorhaditis elegans, DYF-1 serves as an essential activator for an anterograde motor OSM-3 of intraflagellar transport (IFT), the ciliogenesis-required motility process that mediates the transport of flagellar precursors and removal of turnover products. In zebrafish and Terahymena DYF-1 influences the cilia tubulin post-translational modification and may have more ubiquitous function in ciliogenesis than OSM-3. Here we address how DYF-1 biochemically interacts with the IFT machinery by using the model organism Chlamydomonas reinhardtii, in which the anterograde IFT does not depend on OSM-3. Our results show that this protein is a stoichiometric component of the IFT particle complex B and interacts directly with complex B subunit IFT46. In concurrence with the established IFT protein nomenclature, DYF-1 is also named IFT70 after the apparent size of the protein. IFT70/CrDYF-1 is essential for the function of IFT in building the flagellum since the flagella of IFT70/CrDYF-1 depleted cells were greatly shortened. Together, these results demonstrate that IFT70/CrDYF-1 is a canonical subunit of IFT particle complex B, and strongly support the hypothesis that the IFT machinery has species- and tissue- specific variations with functional ramifications.
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