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A family of cytokine-inducible inhibitors of signalling

Author

Listed:
  • Robyn Starr

    (*The Walter and Eliza Hall Institute for Medical Research and The Cooperative Research Center for Cellular Growth Factors)

  • Tracy A. Willson

    (*The Walter and Eliza Hall Institute for Medical Research and The Cooperative Research Center for Cellular Growth Factors)

  • Elizabeth M. Viney

    (*The Walter and Eliza Hall Institute for Medical Research and The Cooperative Research Center for Cellular Growth Factors)

  • Leecia J. L. Murray

    (*The Walter and Eliza Hall Institute for Medical Research and The Cooperative Research Center for Cellular Growth Factors)

  • John R. Rayner

    (†The Hanson Centre for Cancer Research, IMVS)

  • Brendan J. Jenkins

    (†The Hanson Centre for Cancer Research, IMVS)

  • Thomas J. Gonda

    (†The Hanson Centre for Cancer Research, IMVS)

  • Warren S. Alexander

    (*The Walter and Eliza Hall Institute for Medical Research and The Cooperative Research Center for Cellular Growth Factors)

  • Donald Metcalf

    (*The Walter and Eliza Hall Institute for Medical Research and The Cooperative Research Center for Cellular Growth Factors)

  • Nicos A. Nicola

    (*The Walter and Eliza Hall Institute for Medical Research and The Cooperative Research Center for Cellular Growth Factors)

  • Douglas J. Hilton

    (*The Walter and Eliza Hall Institute for Medical Research and The Cooperative Research Center for Cellular Growth Factors)

Abstract

Cytokines are secreted proteins that regulate important cellular responses such as proliferation and differentiation1. Key events in cytokine signal transduction are well defined: cytokines induce receptor aggregation, leading to activation of members of the JAK family of cytoplasmic tyrosine kinases. In turn, members of theSTAT family of transcription factors are phosphorylated, dimerize and increase the transcription of genes with STAT recognition sites in their promoters1,2,3,4. Less is known of how cytokine signal transduction is switched off. We have cloned a complementary DNA encoding a protein SOCS-1, containing an SH2-domain, by its ability to inhibit the macrophage differentiation of M1 cells in response to interleukin-6. Expression of SOCS-1 inhibited both interleukin-6-induced receptor phosphorylation and STAT activation. We have also cloned two relatives of SOCS-1, named SOCS-2 and SOCS-3, which together with the previously described CIS (ref. 5) form a new family of proteins. Transcription of all four SOCS genes is increased rapidly in response to interleukin-6, in vitro and in vivo, suggesting they may act in a classic negative feedback loop to regulate cytokine signal transduction.

Suggested Citation

  • Robyn Starr & Tracy A. Willson & Elizabeth M. Viney & Leecia J. L. Murray & John R. Rayner & Brendan J. Jenkins & Thomas J. Gonda & Warren S. Alexander & Donald Metcalf & Nicos A. Nicola & Douglas J. , 1997. "A family of cytokine-inducible inhibitors of signalling," Nature, Nature, vol. 387(6636), pages 917-921, June.
    • Handle: RePEc:nat:nature:v:387:y:1997:i:6636:d:10.1038_43206
    DOI: 10.1038/43206
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    Cited by:

    1. Edmond M. Linossi & Kunlun Li & Gianluca Veggiani & Cyrus Tan & Farhad Dehkhoda & Colin Hockings & Dale J. Calleja & Narelle Keating & Rebecca Feltham & Andrew J. Brooks & Shawn S. Li & Sachdev S. Sid, 2021. "Discovery of an exosite on the SOCS2-SH2 domain that enhances SH2 binding to phosphorylated ligands," Nature Communications, Nature, vol. 12(1), pages 1-13, December.

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