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.
The RING domain of PIASy is involved in the suppression of bone morphogenetic protein-signaling pathway. Publishing Authors By Initials
The RING domain of PIASy is involved in the suppression of bone morphogenetic protein-signaling pathway. Information
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LANGUAGE: eng
NlmUniqueID: 372516
The RING domain of PIASy is involved in the suppression of bone morphogenetic protein-signaling pathway. Keywords Mesh Terms:
KEYWORDS: Transforming Growth Factor beta
MESH TERMS: metabolism
Chemical & Substance for Abstract: The RING domain of PIASy is involved in the suppression of bone morphogenetic protein-signaling pathway. Information
Substance Name: Luciferases
Registry Number: EC 1.13.12.-
Grant and Affiliation Information for The RING domain of PIASy is involved in the suppression of bone morphogenetic protein-signaling pathway.
AFFILIATION: Department of Immunology, Graduate School of Pharmaceutical Sciences, Hokkaido University, Kita-Ku Kita 12 Nishi 6, Sapporo 060-0812, Japan.
Country: United States
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MEDLINETA: Biochem Biophys Res Commun
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