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TGF-β signalling from cell membrane to nucleus through SMAD proteins

Author

Listed:
  • Carl-Henrik Heldin

    (the Ludwig Institute for Cancer Research)

  • Kohei Miyazono

    (The Cancer Institute)

  • Peter ten Dijke

    (the Ludwig Institute for Cancer Research)

Abstract

The recent identification of the SMAD family of signal transducer proteins has unravelled the mechanisms by which transforming growth factor-β (TGF-β) signals from the cell membrane to the nucleus. Pathway-restricted SMADs are phosphorylated by specific cell-surface receptors that have serine/threonine kinase activity, then they oligomerize with the common mediator Smad4 and translocate to the nucleus where they direct transcription to effect the cell's response to TGF-β. Inhibitory SMADs have been identified that block the activation of these pathway-restricted SMADs.

Suggested Citation

  • Carl-Henrik Heldin & Kohei Miyazono & Peter ten Dijke, 1997. "TGF-β signalling from cell membrane to nucleus through SMAD proteins," Nature, Nature, vol. 390(6659), pages 465-471, December.
    • Handle: RePEc:nat:nature:v:390:y:1997:i:6659:d:10.1038_37284
    DOI: 10.1038/37284
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    Cited by:

    1. Zhanmei Zhou & Zheng Hu & Mei Li & Fengxin Zhu & Hao Zhang & Jing Nie & Jun Ai, 2016. "QiShenYiQi Attenuates Renal Interstitial Fibrosis by Blocking the Activation of β-Catenin," PLOS ONE, Public Library of Science, vol. 11(9), pages 1-18, September.

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