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ZFIN ID: ZDB-PUB-140513-410
TTC26/DYF13 is an intraflagellar transport protein required for transport of motility-related proteins into flagella
Ishikawa, H., Ide, T., Yagi, T., Jiang, X., Hirono, M., Sasaki, H., Yanagisawa, H., Wemmer, K.A., Stainier, D.Y., Qin, H., Kamiya, R., Marshall, W.F.
Date: 2014
Source: eLIFE   3: e01566 (Journal)
Registered Authors: Stainier, Didier
Keywords: Chlamydomonas, axoneme, dynein, flagella
MeSH Terms:
  • Algal Proteins/genetics
  • Algal Proteins/metabolism*
  • Animals
  • Carrier Proteins/genetics
  • Carrier Proteins/metabolism*
  • Cell Line
  • Cell Movement*
  • Chlamydomonas reinhardtii/genetics
  • Chlamydomonas reinhardtii/metabolism*
  • Cilia/metabolism*
  • Embryo, Nonmammalian/metabolism
  • Flagella/metabolism*
  • Gene Expression Regulation, Developmental
  • Gene Knockdown Techniques
  • Genotype
  • Intracellular Signaling Peptides and Proteins/genetics
  • Intracellular Signaling Peptides and Proteins/metabolism*
  • Mice
  • Mutation
  • Phenotype
  • Plant Proteins/genetics
  • Plant Proteins/metabolism*
  • Protein Transport
  • Transfection
  • Zebrafish
  • Zebrafish Proteins/genetics
  • Zebrafish Proteins/metabolism*
PubMed: 24596149 Full text @ Elife
Cilia/flagella are assembled and maintained by the process of intraflagellar transport (IFT), a highly conserved mechanism involving more than 20 IFT proteins. However, the functions of individual IFT proteins are mostly unclear. To help address this issue, we focused on a putative IFT protein TTC26/DYF13. Using live imaging and biochemical approaches we show that TTC26/DYF13 is an IFT complex B protein in mammalian cells and Chlamydomonas reinhardtii. Knockdown of TTC26/DYF13 in zebrafish embryos or mutation of TTC26/DYF13 in C. reinhardtii, produced short cilia with abnormal motility. Surprisingly, IFT particle assembly and speed were normal in dyf13 mutant flagella, unlike in other IFT complex B mutants. Proteomic and biochemical analyses indicated a particular set of proteins involved in motility was specifically depleted in the dyf13 mutant. These results support the concept that different IFT proteins are responsible for different cargo subsets, providing a possible explanation for the complexity of the IFT machinery.