Phosphorylation of Erp1 by p90rsk is required for cytostatic factor arrest in Xenopus laevis eggs

Tomoko Nishiyama, Keita Ohsumi () and Takeo Kishimoto
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Tomoko Nishiyama: Laboratory of Cell and Developmental Biology, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, 4259 Nagatsuta, Midori-ku, Yokohama 226-8501, Japan
Keita Ohsumi: Laboratory of Cell and Developmental Biology, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, 4259 Nagatsuta, Midori-ku, Yokohama 226-8501, Japan
Takeo Kishimoto: Laboratory of Cell and Developmental Biology, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, 4259 Nagatsuta, Midori-ku, Yokohama 226-8501, Japan

Nature, 2007, vol. 446, issue 7139, 1096-1099

Abstract: Vertebrate oocytes are arrested in meiosis II until fertilization. This is one of two papers that link two previously known regulators of this arrest: the kinase Rsk that is activated by the Mos–MAPK pathway, directly phosphorylates Xerp1/Emi2 and thereby promotes its ability to inhibit the anaphase promoting complex APC/C.

Date: 2007
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DOI: 10.1038/nature05696

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