Conserved role for 14-3-3epsilon downstream of type I TGFbeta receptors.
Schistosoma mansoni receptor kinase-1 (SmRK1) is a divergent type I transforming growth factor beta (TGFbeta) receptor on the surface of adult parasites. Using the intracellular domain of SmRK1 as bait in a yeast two-hybrid screen we identified an interaction with S. mansoni 14-3-3epsilon. The interaction which is phosphorylation-dependent is not ... specific to schistosomes since 14-3-3epsilon also binds to TbetaRI, the human type I TGFbeta receptor. 14-3-3epsilon enhances TGFbeta-mediated signaling by TbetaRI and is the first TbetaRI-interacting non-Smad protein identified that positively regulates this receptor. The interaction of 14-3-3epsilon with schistosome and human TbetaRI suggests a conserved, but previously unappreciated, role for this protein in TGFbeta signaling pathways.
Mesh Terms:
14-3-3 Proteins, Activin Receptors, Type I, Amino Acid Sequence, Animals, COS Cells, DNA, Complementary, DNA-Binding Proteins, Dose-Response Relationship, Drug, Helminth Proteins, Humans, Molecular Sequence Data, Phosphorylation, Plasmids, Precipitin Tests, Protein Binding, Protein Structure, Tertiary, Protein-Serine-Threonine Kinases, Receptors, Cell Surface, Receptors, Transforming Growth Factor beta, Schistosoma, Sequence Homology, Amino Acid, Signal Transduction, Smad Proteins, Trans-Activators, Two-Hybrid System Techniques, Tyrosine 3-Monooxygenase
14-3-3 Proteins, Activin Receptors, Type I, Amino Acid Sequence, Animals, COS Cells, DNA, Complementary, DNA-Binding Proteins, Dose-Response Relationship, Drug, Helminth Proteins, Humans, Molecular Sequence Data, Phosphorylation, Plasmids, Precipitin Tests, Protein Binding, Protein Structure, Tertiary, Protein-Serine-Threonine Kinases, Receptors, Cell Surface, Receptors, Transforming Growth Factor beta, Schistosoma, Sequence Homology, Amino Acid, Signal Transduction, Smad Proteins, Trans-Activators, Two-Hybrid System Techniques, Tyrosine 3-Monooxygenase
FEBS Lett.
Date: Feb. 09, 2001
PubMed ID: 11172812
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