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

CH Heldin, K Miyazono, P Ten Dijke - Nature, 1997 - nature.com
CH Heldin, K Miyazono, P Ten Dijke
Nature, 1997nature.com
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 …
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.
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