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

TGF-β signalling from cell membrane to nucleus through SMAD proteins 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Nature Springer Journals

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

Nature , Volume 390 (6659) – Dec 4, 1997

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References (108)

Publisher
Springer Journals
Copyright
Copyright © 1997 by Macmillan Magazines Ltd.
Subject
Science, Humanities and Social Sciences, multidisciplinary; Science, Humanities and Social Sciences, multidisciplinary; Science, multidisciplinary
ISSN
0028-0836
eISSN
1476-4687
DOI
10.1038/37284
Publisher site
See Article on Publisher Site

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.

Journal

NatureSpringer Journals

Published: Dec 4, 1997

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