TGF-beta signalling from cell membrane to nucleus through SMAD proteins.
Heldin, Carl-Henrik; Miyazono, Kohei; Dijke, Peter ten
[Article] Nature. 390(6659):465-471, December 4, 1997.

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The recent identification of the SMAD family of signal transducer proteins has unravelled the mechanisms by which transforming growth factor-beta (TGF-beta) 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-beta. Inhibitory SMADs have been identified that block the activation of these pathway-restricted SMADs.

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