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- W94450341 abstract "Regulator of G protein signaling RGS3 belongs to a family of RGS proteins that contain the homologous RGS domain which binds the alpha subunits of heterotrimeric G proteins and accelerates their GTPase activity. Through this mechanism RGS3 regulates the signaling mediated by a variety of Gq and Gi coupled receptors. In this study, we found that RGS3 interacts with the novel partners, Smad2, Smad3 and Smad4 - the transcription factors that are activated through a transforming growth factor-beta (TGF-beta) receptor signaling. This interaction is mediated by Smad's Mad homology domain 2 (MH2) and by the region of RGS3 outside of the RGS domain. Overexpression of RGS3 results in inhibition of Smad-mediated gene transcription. RGS3 does not affect TGF-beta - induced Smad phosphorylation, but it prevents heteromerization of Smad3 with Smad4, which is required for Smad's transcriptional activity. Functionally, this translates to inhibition of TGF-beta – induced myofibroblast differentiation by adenovirus-mediated overexpression of RGS3. In conclusion, this study identifies a novel, non-canonical role of RGS3 in regulation of TGF-beta signaling through its interaction with Smad transcription factors." @default.
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- W94450341 date "2008-03-01" @default.
- W94450341 modified "2023-10-18" @default.
- W94450341 title "Regulation of TGF‐beta signaling by RGS3" @default.
- W94450341 doi "https://doi.org/10.1096/fasebj.22.1_supplement.1044.9" @default.
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