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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

Authors

  • Griswold-Prenner I
  • Kamibayashi C
  • Maruoka EM
  • Mumby MC
  • Derynck R

Journal

Molecular and cellular biology

Publication Data

November 23, 1998

Associated Grants

  • Agency: NCI NIH HHS, Id: CA63101
  • Agency: NIGMS NIH HHS, Id: GM49505

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