PUBLICATION

TTC26/DYF13 is an intraflagellar transport protein required for transport of motility-related proteins into flagella

Authors
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.
ID
ZDB-PUB-140513-410
Date
2014
Source
eLIFE   3: e01566 (Journal)
Registered Authors
Stainier, Didier
Keywords
Chlamydomonas, axoneme, dynein, flagella
MeSH Terms
  • Cilia/metabolism*
  • Chlamydomonas reinhardtii/genetics
  • Chlamydomonas reinhardtii/metabolism*
  • Flagella/metabolism*
  • Plant Proteins/genetics
  • Plant Proteins/metabolism*
  • Transfection
  • Embryo, Nonmammalian/metabolism
  • Cell Movement*
  • Algal Proteins/genetics
  • Algal Proteins/metabolism*
  • Intracellular Signaling Peptides and Proteins/genetics
  • Intracellular Signaling Peptides and Proteins/metabolism*
  • Mice
  • Zebrafish
  • Zebrafish Proteins/genetics
  • Zebrafish Proteins/metabolism*
  • Carrier Proteins/genetics
  • Carrier Proteins/metabolism*
  • Gene Expression Regulation, Developmental
  • Phenotype
  • Animals
  • Genotype
  • Cell Line
  • Gene Knockdown Techniques
  • Mutation
  • Protein Transport
PubMed
24596149 Full text @ Elife
Abstract
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.
Errata / Notes
This article is corrected by ZDB-PUB-220906-8.
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