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Vol. 13, Issue 7, 2289-2300, July 2002
and
*Departments of Pathology and Microbiology, and Immunology,
Stanford University School of Medicine, Stanford, California 94305; and
In budding yeast, the Cdc14p phosphatase activates mitotic exit by
dephosphorylation of specific cyclin-dependent kinase (Cdk) substrates
and seems to be regulated by sequestration in the nucleolus until its
release in mitosis. Herein, we have analyzed the two human homologs of
Cdc14p, hCdc14A and hCdc14B. We demonstrate that the human Cdc14A
phosphatase is selective for Cdk substrates in vitro and that although
the protein abundance and intrinsic phosphatase activity of hCdc14A and
B vary modestly during the cell cycle, their localization is cell cycle
regulated. hCdc14A dynamically localizes to interphase but not mitotic
centrosomes, and hCdc14B localizes to the interphase nucleolus. These
distinct patterns of localization suggest that each isoform of human
Cdc14 likely regulates separate cell cycle events. In addition, hCdc14A overexpression induces the loss of the pericentriolar markers pericentrin and Department of Biochemistry, Purdue University, West
Lafayette, Indiana 47907
-tubulin from centrosomes. Overproduction of hCdc14A
also causes mitotic spindle and chromosome segregation defects,
defective karyokinesis, and a failure to complete cytokinesis. Thus,
the hCdc14A phosphatase appears to play a role in the regulation of the
centrosome cycle, mitosis, and cytokinesis, thereby influencing chromosome partitioning and genomic stability in human cells.
Corresponding author. E-mail address:
pjackson{at}stanford.edu.
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