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- W1840163537 endingPage "4369" @default.
- W1840163537 startingPage "4359" @default.
- W1840163537 abstract "Smad proteins transduce signals from transforming growth factor-β (TGF-β) 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-β. 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." @default.
- W1840163537 created "2016-06-24" @default.
- W1840163537 creator A5033277087 @default.
- W1840163537 creator A5072088923 @default.
- W1840163537 creator A5084535456 @default.
- W1840163537 date "2001-12-15" @default.
- W1840163537 modified "2023-10-17" @default.
- W1840163537 title "Smad regulation in TGF-β signal transduction" @default.
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