Broad Specificity in Binding of NIPP-1, Nuclear Inhibitor of Protein Phosphatase-1, to PP1 Isoforms in Vivo

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著者

    • KIM SEI-EUN
    • Division of Biochemical Oncology and Immunology, Institute for Genetic Medicine, Hokkaido University
    • SHIMA HIROSHI
    • Division of Biochemical Oncology and Immunology, Institute for Genetic Medicine, Hokkaido University
    • NAKAMURA KOJI
    • Division of Biochemical Oncology and Immunology, Institute for Genetic Medicine, Hokkaido University
    • KIKUCHI KUNIMI
    • Division of Biochemical Oncology and Immunology, Institute for Genetic Medicine, Hokkaido University

抄録

Protein phosphatase type-1 (PP1), one of the most abundant Ser/Thr protein phosphatases, plays a central role in the regulation of various cell functions. Almost all the PP1 molecules exist as holoenzymes in vivo consisting of a catalytic subunit (PP1C) and a variable regulatory subunit that regulates substrate specificity and/or subcellular localization. In order to clarify fine regulation of PP1, we overexpressed a nuclear inhibitor of PP1 (NIPP-1) in a Flag-tagged form in mammalian cells. The Flag-tagged NIPP-1 was found to be immunoprecipitated with three isoforms of PP1C, namely, PP1α, PP1γ1, and PP1δ with a similar efficiency, suggesting that NIPP-1 makes a complex with the PP1C through the region conserved among the three isoforms. These results suggested that NIPP-1 can be involved in the regulation of various PP1 holoenzymes in vivo.

収録刊行物

  • THE TOHOKU JOURNAL OF EXPERIMENTAL MEDICINE

    THE TOHOKU JOURNAL OF EXPERIMENTAL MEDICINE 191(1), 39-45, 2000-05-01

    東北ジャーナル刊行会

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各種コード

  • NII論文ID(NAID)
    10013014995
  • NII書誌ID(NCID)
    AA00863920
  • 本文言語コード
    ENG
  • 資料種別
    ART
  • ISSN
    00408727
  • データ提供元
    CJP書誌  J-STAGE 
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