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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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The RING domain of PIASy is involved in the suppression of bone morphogenetic protein-signaling pathway.

Bone morphogenetic proteins (BMPs) play central roles in differentiation, development, and physiologic tissue remodeling. Recently, we have demonstrated that a protein inhibitor of activated STAT, PIASy, suppresses TGF-beta signaling by interacting with Sma and MAD-related protein 3 (Smad3). In this study, we examined a PIASy-dependent inhibitory effect on BMP signaling. PIASy expression was induced by BMP-2 stimulation and suppressed BMP-2-dependent Smad activity in hepatoma cells. Furthermore, BMP-2- regulated Smads directly bound to PIASy. We also demonstrated that the RING domain of PIASy played an important role in PIASy- mediated suppression of Smad activity. We here provide evidence that the inhibitory action of PIASy on BMP- regulated Smad activity was due to direct physical interactions between Smads and PIASy through its RING domain.[1]

References

  1. The RING domain of PIASy is involved in the suppression of bone morphogenetic protein-signaling pathway. Imoto, S., Sugiyama, K., Yamamoto, T., Matsuda, T. Biochem. Biophys. Res. Commun. (2004) [Pubmed]
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