A new protein containing an SH2 domain that inhibits JAK kinases

Takaho A. Endo, Masaaki Masuhara, Masahiro Yokouchi, Ritsu Suzuki, Hiroshi Sakamoto, Kaoru Mitsui, Akira Matsumoto, Shyu Tanimura, Motoaki Ohtsubo, Hiroyuki Misawa, Tadaaki Miyazaki, Nogueira Leonor, Tadatsugu Taniguchi, Takashi Fujita, Yuzuru Kanakura, Seturo Komiya and Akihiko Yoshimura ()
Additional contact information
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
Ritsu Suzuki: *Institute of Life Science, 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

Nature, 1997, vol. 387, issue 6636, 921-924

Abstract: 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.

Date: 1997
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DOI: 10.1038/43213

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