Regulation of the Anaphase-promoting Complex by the Dual Specificity Phosphatase Human Cdc14a

Two forms of the anaphase-promoting complex (APC) mediate the degradation of critical cell cycle regulators. APCCdc20 promotes sister-chromatid separation by ubiquitinating securin, whereas APCCdh1 ubiquitinates mitotic cyclins, allowing the exit from mitosis. Here we show that phosphorylation of hu...

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Bibliographic Details
Published in:The Journal of biological chemistry 2001-12, Vol.276 (51), p.48237-48242
Main Authors: Bembenek, Joshua, Yu, Hongtao
Format: Article
Language:English
Subjects:
anaphase-promoting complex
Anaphase-Promoting Complex-Cyclosome
Cdc14a protein
Cdc2 protein
CDC2 Protein Kinase - metabolism
Cdh1 protein
Centrosome - enzymology
centrosomes
Cyclin B - metabolism
Cyclin B1
HeLa Cells
Humans
Ligases - metabolism
Ligases - physiology
Phosphoric Monoester Hydrolases - physiology
Phosphorylation
Protein Tyrosine Phosphatases
securin
Substrate Specificity
Ubiquitin-Protein Ligase Complexes
Ubiquitin-Protein Ligases
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Summary:Two forms of the anaphase-promoting complex (APC) mediate the degradation of critical cell cycle regulators. APCCdc20 promotes sister-chromatid separation by ubiquitinating securin, whereas APCCdh1 ubiquitinates mitotic cyclins, allowing the exit from mitosis. Here we show that phosphorylation of human Cdh1 (hCdh1) by cyclin B-Cdc2 alters the conformation of hCdh1 and prevents it from activating APC. A human homologue of yeast Cdc14, human Cdc14a (hCdc14a), dephosphorylates hCdh1 and activates APCCdh1. In contrast, hCdc14a does not affect the activity of APCCdc20. hCdc14a is a major phosphatase for hCdh1 and localizes to centrosomes in HeLa cells. Therefore, hCdc14a may promote the activation of APCCdh1and exit from mitosis in mammalian cells.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M108126200