TGF-beta-induced phosphorylation of Smad3 regulates its interaction with coactivator p300/CREB-binding protein.

@article{Shen1998TGFbetainducedPO,
  title={TGF-beta-induced phosphorylation of Smad3 regulates its interaction with coactivator p300/CREB-binding protein.},
  author={Xiaoying Shen and Patrick Pei-chih Hu and Nicole T. Liberati and Michael B. Datto and Joshua P. Frederick and X F Wang},
  journal={Molecular biology of the cell},
  year={1998},
  volume={9 12},
  pages={
          3309-19
        }
}
Smads are intermediate effector proteins that transduce the TGF-beta signal from the plasma membrane to the nucleus, where they participate in transactivation of downstream target genes. We have shown previously that coactivators p300/CREB-binding protein are involved in TGF-beta-mediated transactivation of two Cdk inhibitor genes, p21 and p15. Here we examined the possibility that Smads function to regulate transcription by directly interacting with p300/CREB-binding protein. We show that… CONTINUE READING
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