Phosphorylation of SAS-6 by ZYG-1 is critical for centriole formation in C. elegans embryos

Dev Cell. 2009 Dec;17(6):900-7. doi: 10.1016/j.devcel.2009.11.002.

Abstract

Despite being essential for proper cell division, the mechanisms governing centrosome duplication are incompletely understood and represent an important open question in cell biology. Formation of a new centriole next to each existing one is critical for centrosome duplication. In Caenorhabditis elegans embryos, the proteins SPD-2, ZYG-1, SAS-6, SAS-5, and SAS-4 are essential for centriole formation, but the mechanisms underlying their requirement remain unclear. Here, we demonstrate that the kinase ZYG-1 phosphorylates the coiled-coil protein SAS-6 at serine 123 in vitro. Importantly, we show that this phosphorylation event is crucial for centriole formation in vivo. Furthermore, we establish that such phosphorylation ensures the maintenance of SAS-6 at the emerging centriole. Overall, our findings establish that phosphorylation of the evolutionarily conserved protein SAS-6 is critical for centriole formation and thus for faithful cell division.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Caenorhabditis elegans / cytology*
  • Caenorhabditis elegans / metabolism*
  • Caenorhabditis elegans Proteins / metabolism*
  • Cell Cycle Proteins / metabolism*
  • Centrioles / metabolism*
  • Phosphorylation
  • Protein Kinases / metabolism*

Substances

  • Caenorhabditis elegans Proteins
  • Cell Cycle Proteins
  • SAS-6 protein, C elegans
  • SPD-2 protein, C elegans
  • Protein Kinases
  • zyg-1 protein, C elegans