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COMMENTARY |
Ludwig Institute for Cancer Research, Box 595, SE-751 24 Uppsala, Sweden
Corresponding author (e-mail: Aris.Moustakas{at}LICR.uu.se)
Smad proteins transduce signals from transforming growth factor-ß (TGF-ß) 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-ß. 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.
Key words: Phosphorylation, Signal transduction, Smad, Transforming growth factor-ß, Ubiquitination
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