Published online May 5, 2008
doi:10.1083/jcb.200710127
The Journal of Cell Biology, Vol. 181, No. 3, 475-483
The Rockefeller University Press, 0021-9525 $30.00
© 2008 Wu et al.
Cdc14B depletion leads to centriole amplification, and its overexpression prevents unscheduled centriole duplication
Jun Wu1,
Hyekyung P. Cho1,
David B. Rhee1,3,
Dabney K. Johnson1,
John Dunlap2,
Yie Liu3, and
Yisong Wang1
1 Biosciences Division, Oak Ridge National Laboratory, Oak Ridge, TN 37831
2 Microscopy Facility, Division of Biology, University of Tennessee, Knoxville, TN 37996
3 Laboratory of Molecular Gerontology, Gerontology Research Center, National Institute on Aging, Baltimore, MD 21224
Correspondence to Y. Wang: ywa{at}ornl.gov; or Y. Liu: liuyie{at}grc.nia.nih.gov
Centrosome duplication is tightly controlled in coordination with DNA replication. The molecular mechanism of centrosome duplication remains unclear. Previous studies found that a fraction of human proline-directed phosphatase Cdc14B associates with centrosomes. However, Cdc14B's involvement in centrosome cycle control has never been explored. Here, we show that depletion of Cdc14B by RNA interference leads to centriole amplification in both HeLa and normal human fibroblast BJ and MRC-5 cells. Induction of Cdc14B expression through a regulatable promoter significantly attenuates centriole amplification in prolonged S phase–arrested cells and proteasome inhibitor Z-L3VS–treated cells. This inhibitory function requires centriole-associated Cdc14B catalytic activity. Together, these results suggest a potential function for Cdc14B phosphatase in maintaining the fidelity of centrosome duplication cycle.
J. Wu and H.P. Cho contributed equally to this paper.
Abbreviations used in this paper: DOX, doxycycline; HU, hydroxyurea; shRNA, small hairpin RNA.

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