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

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

Kitagawa, Daiju  
•
Busso, Coralie  
•
Fluckiger, Isabelle
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2009
Developmental Cell

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. 2009 Elsevier Inc. All rights reserved

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Type
research article
DOI
10.1016/j.devcel.2009.11.002
Web of Science ID

WOS:000273616800018

Author(s)
Kitagawa, Daiju  
Busso, Coralie  
Fluckiger, Isabelle
Gönczy, Pierre  
Date Issued

2009

Publisher

Cell Press - Elsevier

Published in
Developmental Cell
Volume

17

Issue

6

Start page

900

End page

7

Subjects

Centrosome Duplication

•

Caenorhabditis-Elegans

•

Protein Spd-2

•

Human-Cells

•

Procentriole

•

Recruitment

•

Biogenesis

•

Encodes

•

Cycle

Editorial or Peer reviewed

REVIEWED

Written at

EPFL

EPFL units
UPGON  
Available on Infoscience
February 3, 2010
Use this identifier to reference this record
https://infoscience.epfl.ch/handle/20.500.14299/46417
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