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PMID:9311995
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| Citation |
Nakao, A, Imamura, T, Souchelnytskyi, S, Kawabata, M, Ishisaki, A, Oeda, E, Tamaki, K, Hanai, J, Heldin, CH, Miyazono, K and ten Dijke, P (1997) TGF-beta receptor-mediated signalling through Smad2, Smad3 and Smad4. EMBO J. 16:5353-62 |
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| Abstract |
Smad family members are newly identified essential intracellular signalling components of the transforming growth factor-beta (TGF-beta) superfamily. Smad2 and Smad3 are structurally highly similar and mediate TGF-beta signals. Smad4 is distantly related to Smads 2 and 3, and forms a heteromeric complex with Smad2 after TGF-beta or activin stimulation. Here we show that Smad2 and Smad3 interacted with the kinase-deficient TGF-beta type I receptor (TbetaR)-I after it was phosphorylated by TbetaR-II kinase. TGF-beta1 induced phosphorylation of Smad2 and Smad3 in Mv1Lu mink lung epithelial cells. Smad4 was found to be constitutively phosphorylated in Mv1Lu cells, the phosphorylation level remaining unchanged upon TGF-beta1 stimulation. Similar results were obtained using HSC4 cells, which are also growth-inhibited by TGF-beta. Smads 2 and 3 interacted with Smad4 after TbetaR activation in transfected COS cells. In addition, we observed TbetaR-activation-dependent interaction between Smad2 and Smad3. Smads 2, 3 and 4 accumulated in the nucleus upon TGF-beta1 treatment in Mv1Lu cells, and showed a synergistic effect in a transcriptional reporter assay using the TGF-beta-inducible plasminogen activator inhibitor-1 promoter. Dominant-negative Smad3 inhibited the transcriptional synergistic response by Smad2 and Smad4. These data suggest that TGF-beta induces heteromeric complexes of Smads 2, 3 and 4, and their concomitant translocation to the nucleus, which is required for efficient TGF-beta signal transduction. |
| Links |
PubMed PMC1170167 Online version:10.1093/emboj/16.17.5353 |
| Keywords |
Activin Receptors, Type I; Amino Acid Sequence; Animals; Antibody Specificity; Biological Transport; COS Cells; Cell Nucleus/metabolism; DNA-Binding Proteins/immunology; DNA-Binding Proteins/metabolism; Epithelial Cells; Genes, Reporter; Humans; Lung/cytology; Mink; Models, Biological; Molecular Sequence Data; Phosphorylation; Protein Binding; Protein-Serine-Threonine Kinases/metabolism; Receptors, Transforming Growth Factor beta/metabolism; Signal Transduction; Smad2 Protein; Smad3 Protein; Smad4 Protein; Trans-Activators/immunology; Trans-Activators/metabolism; Transcription, Genetic; Tumor Cells, Cultured |
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