Mechanism of forming the nine-fold centriole structure

September 13, 2022

A new mechanism to determine the shape of centrioles essential to form cytoskeleton structures

A research group at Hosei University, in collaboration with researchers at Paul Scherrer Institute (Switzerland) and the RIKEN CSRS, discovered a new mechanism for forming centrioles, the core structure of centrosomes. The centriole has a nonagonal structure made of nine protein filaments, whose shape has an essential role as the cast of the cilia. Previous studies revealed that the coordination of the cartwheel-like skeletal structure and another unknown mechanism determines the centriole’s shape. Using a single-cell model organism, Chlamydomonas, the collaborative research group revealed that the protein Bld10p/Cep135 links between microtubules to play a crucial role different from that of the cartwheel. These findings have provided new insights into the mechanism of microtubule assembly, which had been unknown previously.

Original article

The EMBO Journal doi:10.15252/embj.2020104582

A. Noga, M. Horii, Y. Goto, K. Toyooka, T. Ishikawa, M. Hirono,

"Bld10p/Cep135 determines the number of triplets in the centriole independently of the cartwheel".

Contact

Kiminori Toyooka
Senior Technical Scientist
Mass Spectrometry and Microscopy Unit