Cdc14B depletion leads to centriole amplification, and its overexpression prevents unscheduled centriole duplication.
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-L(3)VS-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.
Wu
Jun
J
Biosciences Division, Oak Ridge National Laboratory, Oak Ridge, TN 37831, USA.
Cho
Hyekyung P
HP
Rhee
David B
DB
Johnson
Dabney K
DK
Dunlap
John
J
Liu
Yie
Y
Wang
Yisong
Y
D000818:Animals; D002453:Cell Cycle / Q000502:physiology; D002478:Cells, Cultured; D002502:Centrioles / Q000378:metabolism*; D054637:Dual-Specificity Phosphatases / Q000235:genetics / Q000378:metabolism*; D005347:Fibroblasts / Q000166:cytology / Q000502:physiology; D005786:Gene Expression Regulation; D006367:HeLa Cells; D006801:Humans; D011401:Promoter Regions, Genetic; D034622:RNA Interference; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism
D011993:Recombinant Fusion Proteins; C474200:CDC14B protein, human; D054637:Dual-Specificity Phosphatases