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Spred is a Sprouty-related suppressor of Ras signalling

Author

Listed:
  • Toru Wakioka

    (Medical Institute of Bioregulation, Kyushu University
    Faculty of Medicine, Kagoshima University
    Institute of Life Science, Kurume University)

  • Atsuo Sasaki

    (Medical Institute of Bioregulation, Kyushu University)

  • Reiko Kato

    (Medical Institute of Bioregulation, Kyushu University
    Institute of Life Science, Kurume University)

  • Takanori Shouda

    (Medical Institute of Bioregulation, Kyushu University)

  • Akira Matsumoto

    (Medical Institute of Bioregulation, Kyushu University)

  • Kanta Miyoshi

    (Medical Institute of Bioregulation, Kyushu University
    Faculty of Medicine, Kagoshima University)

  • Makoto Tsuneoka

    (Institute of Life Science, Kurume University)

  • Setsuro Komiya

    (Faculty of Medicine, Kagoshima University)

  • Roland Baron

    (Yale University School of Medicine)

  • Akihiko Yoshimura

    (Medical Institute of Bioregulation, Kyushu University
    Institute of Life Science, Kurume University)

Abstract

Cellular proliferation, and differentiation of cells in response to extracellular signals, are controlled by the signal transduction pathway of Ras, Raf and MAP (mitogen-activated protein) kinase. The mechanisms that regulate this pathway are not well known. Here we describe two structurally similar tyrosine kinase substrates, Spred-1 and Spred-2. These two proteins contain a cysteine-rich domain related to Sprouty (the SPR domain) at the carboxy terminus. In Drosophila, Sprouty inhibits the signalling by receptors of fibroblast growth factor (FGF) and epidermal growth factor (EGF) by suppressing the MAP kinase pathway2,3,4,5,6,7. Like Sprouty, Spred inhibited growth-factor-mediated activation of MAP kinase. The Ras–MAP kinase pathway is essential in the differentiation of neuronal cells and myocytes. Expression of a dominant negative form of Spred and Spred-antibody microinjection revealed that endogenous Spred regulates differentiation in these types of cells. Spred constitutively associated with Ras but did not prevent activation of Ras or membrane translocation of Raf. Instead, Spred inhibited the activation of MAP kinase by suppressing phosphorylation and activation of Raf. Spred may represent a class of proteins that modulate Ras–Raf interaction and MAP kinase signalling.

Suggested Citation

  • Toru Wakioka & Atsuo Sasaki & Reiko Kato & Takanori Shouda & Akira Matsumoto & Kanta Miyoshi & Makoto Tsuneoka & Setsuro Komiya & Roland Baron & Akihiko Yoshimura, 2001. "Spred is a Sprouty-related suppressor of Ras signalling," Nature, Nature, vol. 412(6847), pages 647-651, August.
    • Handle: RePEc:nat:nature:v:412:y:2001:i:6847:d:10.1038_35088082
    DOI: 10.1038/35088082
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    Cited by:

    1. Lianjun Zhang & Le Xuan Truong Nguyen & Ying-Chieh Chen & Dijiong Wu & Guerry J. Cook & Dinh Hoa Hoang & Casey J. Brewer & Xin He & Haojie Dong & Shu Li & Man Li & Dandan Zhao & Jing Qi & Wei-Kai Hua , 2021. "Targeting miR-126 in inv(16) acute myeloid leukemia inhibits leukemia development and leukemia stem cell maintenance," Nature Communications, Nature, vol. 12(1), pages 1-17, December.

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