Physical and functional interactions between type I transforming growth factor beta receptors and Balpha, a WD-40 repeat subunit of phosphatase 2A.
We have previously shown that a WD-40 repeat protein, TRIP-1, associates with the type II transforming growth factor beta (TGF-beta) receptor. In this report, we show that another WD-40 repeat protein, the Balpha subunit of protein phosphatase 2A, associates with the cytoplasmic domain of type I TGF-beta receptors. This association ... depends on the kinase activity of the type I receptor, is increased by coexpression of the type II receptor, which is known to phosphorylate and activate the type I receptor, and allows the type I receptor to phosphorylate Balpha. Furthermore, Balpha enhances the growth inhibition activity of TGF-beta in a receptor-dependent manner. Because Balpha has been characterized as a regulator of phosphatase 2A activity, our observations suggest possible functional interactions between the TGF-beta receptor complex and the regulation of protein phosphatase 2A.
Mesh Terms:
3T3 Cells, Activin Receptors, Type I, Animals, Cell Division, Cross-Linking Reagents, Cyclin A, Gene Expression Regulation, Enzymologic, Genes, Reporter, Membrane Proteins, Mice, Phosphoprotein Phosphatases, Phosphorylation, Protein Kinases, Protein Phosphatase 2, Protein-Serine-Threonine Kinases, Receptors, Transforming Growth Factor beta, Recombinant Fusion Proteins, Signal Transduction
3T3 Cells, Activin Receptors, Type I, Animals, Cell Division, Cross-Linking Reagents, Cyclin A, Gene Expression Regulation, Enzymologic, Genes, Reporter, Membrane Proteins, Mice, Phosphoprotein Phosphatases, Phosphorylation, Protein Kinases, Protein Phosphatase 2, Protein-Serine-Threonine Kinases, Receptors, Transforming Growth Factor beta, Recombinant Fusion Proteins, Signal Transduction
Mol. Cell. Biol.
Date: Nov. 01, 1998
PubMed ID: 9774674
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