scholarly journals Author response: TTC26/DYF13 is an intraflagellar transport protein required for transport of motility-related proteins into flagella

2014 ◽  
Author(s):  
Hiroaki Ishikawa ◽  
Takahiro Ide ◽  
Toshiki Yagi ◽  
Xue Jiang ◽  
Masafumi Hirono ◽  
...  
eLife ◽  
2014 ◽  
Vol 3 ◽  
Author(s):  
Hiroaki Ishikawa ◽  
Takahiro Ide ◽  
Toshiki Yagi ◽  
Xue Jiang ◽  
Masafumi Hirono ◽  
...  

eLife ◽  
2014 ◽  
Vol 3 ◽  
Author(s):  
Hiroaki Ishikawa ◽  
Takahiro Ide ◽  
Toshiki Yagi ◽  
Xue Jiang ◽  
Masafumi Hirono ◽  
...  

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.


2018 ◽  
Author(s):  
Michael Taschner ◽  
Anna Lorentzen ◽  
André Mourão ◽  
Toby Collins ◽  
Grace M Freke ◽  
...  

2011 ◽  
Vol 20 (19) ◽  
pp. 3725-3737 ◽  
Author(s):  
J. M. Friedland-Little ◽  
A. D. Hoffmann ◽  
P. J. R. Ocbina ◽  
M. A. Peterson ◽  
J. D. Bosman ◽  
...  

2018 ◽  
Vol 9 (1) ◽  
Author(s):  
Qianmin Wang ◽  
Michael Taschner ◽  
Kristina A. Ganzinger ◽  
Charlotte Kelley ◽  
Alethia Villasenor ◽  
...  

2020 ◽  
Vol 219 (5) ◽  
Author(s):  
PeiQi Li ◽  
Joshua Aaron Lees ◽  
C. Patrick Lusk ◽  
Karin M. Reinisch

A single particle cryo-EM reconstruction of an ∼160-kD N-terminal fragment of the lipid transport protein VPS13 reveals an ∼160-Å long channel lined with hydrophobic residues suitable for solubilizing multiple lipid fatty acid moieties. The structure suggests that VPS13 and related proteins, like the autophagy protein ATG2, can act as bridges between organelle membranes to allow bulk lipid flow between organelles.


Life Sciences ◽  
2020 ◽  
Vol 260 ◽  
pp. 118216
Author(s):  
Vincent Z. Luu ◽  
Albert Z. Luu ◽  
Biswajit Chowdhury ◽  
Omar Elbardisy ◽  
Yi Pan ◽  
...  

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