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.
Pubmed ID: 9774674 RIS Download
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