4.7 Article

Phosphorylation of SAS-6 by ZYG-1 Is Critical for Centriole Formation in C. elegans Embryos

期刊

DEVELOPMENTAL CELL
卷 17, 期 6, 页码 900-907

出版社

CELL PRESS
DOI: 10.1016/j.devcel.2009.11.002

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资金

  1. JSPS
  2. EMBO [ALTF-667-2007]
  3. Oncosuisse [02024-02-2007]
  4. ERC [233335]
  5. European Research Council (ERC) [233335] Funding Source: European Research Council (ERC)

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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.

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