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A new protein containing an SH2 domain that inhibits JAK kinases

Author

Listed:
  • Takaho A. Endo

    (*Institute of Life Science, Kurume University)

  • Masaaki Masuhara

    (*Institute of Life Science, Kurume University)

  • Masahiro Yokouchi

    (*Institute of Life Science, Kurume University
    Kurume University)

  • Ritsu Suzuki

    (*Institute of Life Science, Kurume University
    Kurume University)

  • Hiroshi Sakamoto

    (*Institute of Life Science, Kurume University)

  • Kaoru Mitsui

    (*Institute of Life Science, Kurume University)

  • Akira Matsumoto

    (*Institute of Life Science, Kurume University)

  • Shyu Tanimura

    (*Institute of Life Science, Kurume University)

  • Motoaki Ohtsubo

    (*Institute of Life Science, Kurume University)

  • Hiroyuki Misawa

    (*Institute of Life Science, Kurume University)

  • Tadaaki Miyazaki

    (Faculty of Medicine, University of Tokyo)

  • Nogueira Leonor

    (Faculty of Medicine, University of Tokyo)

  • Tadatsugu Taniguchi

    (Faculty of Medicine, University of Tokyo)

  • Takashi Fujita

    (The Tokyo Metropolitan Institute of Medical Science)

  • Yuzuru Kanakura

    (Osaka University Medical School)

  • Seturo Komiya

    (Kurume University)

  • Akihiko Yoshimura

    (*Institute of Life Science, Kurume University)

Abstract

The proliferation and differentiation of cells of many lineages are regulated by secreted proteins known as cytokines. Cytokines exert their biological effect through binding to cell-surface receptors that are associated with one or more members of the JAK family of cytoplasmic tyrosine kinases. Cytokine-induced receptor dimerization leads to the activation of JAKs, rapid tyrosine-phosphorylation of the cytoplasmic domains, and subsequent recruitment of various signalling proteins, including members of the STAT family of transcription factors, to the receptor complex1,2,3,4,5. Using the yeast two-hybrid system, we have now isolated a new SH2-domain-containing protein, JAB, which is a JAK-binding protein that interacts with the Jak2 tyrosine-kinase JH1 domain6. JAB is structurally related to CIS, a cytokine-inducible SH2 protein7,8. Interaction of JAB with Jak1, Jak2 or Jak3 markedly reduces their tyrosine-kinase activity and suppresses the tyrosine-phosphorylation and activation of STATs. JAB and CIS appear to function as negative regulators in the JAK signalling pathway.

Suggested Citation

  • Takaho A. Endo & Masaaki Masuhara & Masahiro Yokouchi & Ritsu Suzuki & Hiroshi Sakamoto & Kaoru Mitsui & Akira Matsumoto & Shyu Tanimura & Motoaki Ohtsubo & Hiroyuki Misawa & Tadaaki Miyazaki & Noguei, 1997. "A new protein containing an SH2 domain that inhibits JAK kinases," Nature, Nature, vol. 387(6636), pages 921-924, June.
    • Handle: RePEc:nat:nature:v:387:y:1997:i:6636:d:10.1038_43213
    DOI: 10.1038/43213
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    Cited by:

    1. Samira Schiefer & Benjamin G. Hale, 2024. "Proximal protein landscapes of the type I interferon signaling cascade reveal negative regulation by PJA2," Nature Communications, Nature, vol. 15(1), pages 1-19, December.
    2. Jiajia Wang & Jiaying Wang & Wenxiang Hong & Lulu Zhang & Liqian Song & Qi Shi & Yanfei Shao & Guifeng Hao & Chunyan Fang & Yueping Qiu & Lijun Yang & Zhaoxu Yang & Jincheng Wang & Ji Cao & Bo Yang & , 2021. "Optineurin modulates the maturation of dendritic cells to regulate autoimmunity through JAK2-STAT3 signaling," Nature Communications, Nature, vol. 12(1), pages 1-15, December.

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