
pmid: 11243848
Regulation of subcellular localization of Smad proteins is supposed to be critical for the effective initiation and maintenance of TGF-beta signaling. Recently, Smad anchor for receptor activation (SARA) has been identified as a Smad2 binding protein. SARA regulates the subcellular localization of Smad2 and is required for TGF-beta/Smad2-mediated signaling. In this study, we determined whether the interaction between SARA and Smad3 is essential for TGF-beta/Smad3-mediated signaling. We found that a mutant Smad3 (Smad3NS) that lacked the binding to SARA was phosphorylated by TGF-beta type I receptor at the similar level to that in wild-type Smad3 (Smad3WT). Smad3NS also formed complexes with Smad4 and translocalized into the nucleus. Moreover, Smad3NS and Smad3WT equally enhanced TGF-beta-induced transcription. Therefore, these findings indicate that, in contrast to SARA/Smad2 interaction, SARA/Smad3 interaction is not essential for TGF-beta/Smad3-mediated signaling.
Cell Nucleus, Transcriptional Activation, Endosomal Sorting Complexes Required for Transport, Macromolecular Substances, Active Transport, Cell Nucleus, Receptor, Transforming Growth Factor-beta Type I, Protein Serine-Threonine Kinases, 540, Phosphoproteins, Transfection, DNA-Binding Proteins, COS Cells, Mutation, Trans-Activators, Animals, Smad3 Protein, Phosphorylation, Carrier Proteins, Activin Receptors, Type I, Receptors, Transforming Growth Factor beta, Signal Transduction
Cell Nucleus, Transcriptional Activation, Endosomal Sorting Complexes Required for Transport, Macromolecular Substances, Active Transport, Cell Nucleus, Receptor, Transforming Growth Factor-beta Type I, Protein Serine-Threonine Kinases, 540, Phosphoproteins, Transfection, DNA-Binding Proteins, COS Cells, Mutation, Trans-Activators, Animals, Smad3 Protein, Phosphorylation, Carrier Proteins, Activin Receptors, Type I, Receptors, Transforming Growth Factor beta, Signal Transduction
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