2024-03-28T19:49:26Zhttps://eprints.lib.hokudai.ac.jp/dspace-oai/requestoai:eprints.lib.hokudai.ac.jp:2115/281162022-11-17T02:08:08Zhdl_2115_20044hdl_2115_124The RING domain of PIASy is involved in the suppression of bone morphogenetic protein-signaling pathway.Imoto, SeiyuSugiyama, KenjiYamamoto, TetsuyaMatsuda, TadashiBMPSmadRING domainPIASyTranscription499.3Bone 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-β 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.ElsevierJournal Articleapplication/pdfhttp://hdl.handle.net/2115/28116https://eprints.lib.hokudai.ac.jp/dspace/bitstream/2115/28116/1/BBRC319-1.pdf0006-291X1090-2104Biochemical and Biophysical Research Communications31912752822004-06-18enginfo:pmid/15158472info:doi/10.1016/j.bbrc.2004.04.161author