A new protein containing an SH2 domain that inhibits JAK kinases View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

1997-06

AUTHORS

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, Akihiko Yoshimura

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. More... »

PAGES

921-924

References to SciGraph publications

Journal

TITLE

Nature

ISSUE

6636

VOLUME

387

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/43213

    DOI

    http://dx.doi.org/10.1038/43213

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1015325599

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/9202126


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