Daiju Kitagawa 2026-11-05
Daiju Kitagawa led work explaining the ninefold organization of centrioles through interactions between SAS-6 molecules. The 2011 study combined structural analysis, biochemical assembly and cellular experiments: rod-shaped dimers associated through their ends, and disrupting the relevant association impaired centriole formation.[ref]
A model built from the related Chlamydomonas reinhardtii protein placed nine dimers in a ring with spokes extending outward. Recombinant protein also formed cartwheel-like assemblies. The work connects a repeated protein structure to the larger geometry of an organelle, rather than treating its symmetry as an unexplained cellular pattern.[ref]
SAS-6 2026-11-05
SAS-6 is a family of scaffold proteins required for normal centriole assembly. Elongated SAS-6 dimers can associate through their head domains to form the central hub and radiating spokes of the centriole cartwheel. This supplies a molecular route from interactions between proteins to the ninefold organization of a much larger organelle.
Daiju Kitagawa and colleagues combined protein structure determination, assembly experiments and cellular perturbations. Their model arranged nine dimers into a ring; electron microscopy of recombinant algal SAS-6 showed cartwheel-like assemblies, while mutations that impaired head-domain association also impaired centriole formation. The isolated structure alone would show a possible geometry; its agreement with assembly and perturbation experiments connects that geometry to function.[ref]