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.
Date: 2010
Source: Molecular biology of the cell   21(15): 2696-2706 (Journal)
Registered Authors:
Keywords: none
MeSH Terms:
  • Algal Proteins/chemistry
  • Algal Proteins/metabolism*
  • Amino Acid Sequence
  • Axoneme/metabolism
  • Axoneme/ultrastructure
  • Chlamydomonas/cytology
  • Chlamydomonas/metabolism*
  • Chlamydomonas/ultrastructure
  • Conserved Sequence/genetics
  • Flagella/metabolism*
  • Flagella/ultrastructure
  • Gene Knockdown Techniques
  • Kinesin/metabolism
  • Molecular Sequence Data
  • Protein Binding
  • Protein Subunits/metabolism
  • Recombinant Proteins/metabolism
PubMed: 20534810 Full text @ Mol. Biol. Cell
Monitoring 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.