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Review
. 2001 Dec;114(Pt 24):4359-69.
doi: 10.1242/jcs.114.24.4359.

Smad regulation in TGF-beta signal transduction

A Moustakas  1 , S Souchelnytskyi, C H Heldin
Affiliations
Review

Smad regulation in TGF-beta signal transduction

A Moustakas et al. J Cell Sci. 2001 Dec.

Abstract

Smad proteins transduce signals from transforming growth factor-beta (TGF-beta) superfamily ligands that regulate cell proliferation, differentiation and death through activation of receptor serine/threonine kinases. Phosphorylation of receptor-activated Smads (R-Smads) leads to formation of complexes with the common mediator Smad (Co-Smad), which are imported to the nucleus. Nuclear Smad oligomers bind to DNA and associate with transcription factors to regulate expression of target genes. Alternatively, nuclear R-Smads associate with ubiquitin ligases and promote degradation of transcriptional repressors, thus facilitating target gene regulation by TGF-beta. Smads themselves can also become ubiquitinated and are degraded by proteasomes. Finally, the inhibitory Smads (I-Smads) block phosphorylation of R-Smads by the receptors and promote ubiquitination and degradation of receptor complexes, thus inhibiting signalling.

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