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

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

  • Kitagawa D Swiss Institute for Experimental Cancer Research (ISREC), School of Life Sciences, Swiss Federal Institute of Technology (EPFL), CH-1015 Lausanne, Switzerland.
  • Busso C
  • Flückiger I
  • Gönczy P
  • 2010-01-12
Published in:
  • Developmental cell. - 2009
Animals
Caenorhabditis elegans
Caenorhabditis elegans Proteins
Cell Cycle Proteins
Centrioles
Phosphorylation
Protein Kinases
English 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.
Language
  • English
Open access status
closed
Identifiers
Persistent URL
https://sonar.ch/global/documents/209751
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