Purification and Molecular Cloning of Plx1, a Cdc25-Regulatory Kinase from <b> <i>Xenopus</i> </b> Egg Extracts
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- Akiko Kumagai
- Division of Biology, 216-76, Howard Hughes Medical Institute, California Institute of Technology, Pasadena, CA 91125, USA.
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- William G. Dunphy
- Division of Biology, 216-76, Howard Hughes Medical Institute, California Institute of Technology, Pasadena, CA 91125, USA.
書誌事項
- 公開日
- 1996-09-06
- DOI
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- 10.1126/science.273.5280.1377
- 公開者
- American Association for the Advancement of Science (AAAS)
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説明
<jats:p> Cdc2, the cyclin-dependent kinase that controls mitosis, is negatively regulated by phosphorylation on its threonine-14 and tyrosine-15 residues. Cdc25, the phosphatase that dephosphorylates both of these residues, undergoes activation and phosphorylation by multiple kinases at mitosis. Plx1, a kinase that associates with and phosphorylates the amino-terminal domain of Cdc25, was purified extensively from <jats:italic>Xenopus</jats:italic> egg extracts. Cloning of its complementary DNA revealed that Plx1 is related to the Polo family of protein kinases. Recombinant Plx1 phosphorylated Cdc25 and stimulated its activity in a purified system. Cdc25 phosphorylated by Plx1 reacted strongly with MPM-2, a monoclonal antibody to mitotic phosphoproteins. These studies indicate that Plx1 may participate in control of mitotic progression. </jats:p>
収録刊行物
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- Science
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Science 273 (5280), 1377-1380, 1996-09-06
American Association for the Advancement of Science (AAAS)
