SAS-6 assembly templated by the lumen of cartwheel-less centrioles precedes centriole duplication

Dev Cell. 2014 Jul 28;30(2):238-45. doi: 10.1016/j.devcel.2014.05.008. Epub 2014 Jul 10.

Abstract

Centrioles are 9-fold symmetric structures duplicating once per cell cycle. Duplication involves self-oligomerization of the centriolar protein SAS-6, but how the 9-fold symmetry is invariantly established remains unclear. Here, we found that SAS-6 assembly can be shaped by preexisting (or mother) centrioles. During S phase, SAS-6 molecules are first recruited to the proximal lumen of the mother centriole, adopting a cartwheel-like organization through interactions with the luminal wall, rather than via their self-oligomerization activity. The removal or release of luminal SAS-6 requires Plk4 and the cartwheel protein STIL. Abolishing either the recruitment or the removal of luminal SAS-6 hinders SAS-6 (or centriole) assembly at the outside wall of mother centrioles. After duplication, the lumen of engaged mother centrioles becomes inaccessible to SAS-6, correlating with a block for reduplication. These results lead to a proposed model that centrioles may duplicate via a template-based process to preserve their geometry and copy number.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Cell Cycle Proteins / chemistry
  • Cell Cycle Proteins / metabolism
  • Cell Line, Tumor
  • Centrioles / metabolism*
  • Humans
  • Protein Binding
  • Protein Multimerization
  • Protein Structure, Tertiary

Substances

  • Cell Cycle Proteins
  • SASS6 protein, human