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http://purl.uniprot.org/citations/9670020http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9670020http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9670020http://www.w3.org/2000/01/rdf-schema#comment"Smad proteins are signal transducers for the members of the transforming growth factor-beta (TGF-beta) superfamily. Here we show that, in the absence TGF-beta stimulation, Smads exist as monomers in vivo. Smad2 and Smad3 form homo-oligomers upon phosphorylation by the constitutively active TGF-beta type I receptor, and this oligomerization does not require Smad4. Major portions of Smad4, Smad6 and Smad7 are also present as monomers in vivo. Analysis using a cross-linking reagent suggested that the Smad2 oligomer induced by receptor activation is a trimer. Studies by gel chromatography demonstrated that the Smad2-Smad4 heteromer is not larger than the Smad2 homomer. Moreover, overexpression of Smad4 prevented Smad2 from forming a homo-oligomer. These findings suggest that Smad2 may form a homotrimer, or heterotrimers with Smad4, which are probably composed of two and one, or one and two molecules of Smad2 and Smad4, respectively, depending on the amount of each protein. Gel-mobility shift assay revealed that the Smad3 homomer and Smad3-Smad4 heteromer constitute DNA-binding complexes. Transition of the Smad proteins from monomers to oligomers is thus a critical event in the signal transduction of the TGF-beta superfamily members."xsd:string
http://purl.uniprot.org/citations/9670020http://purl.org/dc/terms/identifier"doi:10.1093/emboj/17.14.4056"xsd:string
http://purl.uniprot.org/citations/9670020http://purl.org/dc/terms/identifier"doi:10.1093/emboj/17.14.4056"xsd:string
http://purl.uniprot.org/citations/9670020http://purl.uniprot.org/core/author"Inoue H."xsd:string
http://purl.uniprot.org/citations/9670020http://purl.uniprot.org/core/author"Inoue H."xsd:string
http://purl.uniprot.org/citations/9670020http://purl.uniprot.org/core/author"Imamura T."xsd:string
http://purl.uniprot.org/citations/9670020http://purl.uniprot.org/core/author"Imamura T."xsd:string
http://purl.uniprot.org/citations/9670020http://purl.uniprot.org/core/author"Miyazono K."xsd:string
http://purl.uniprot.org/citations/9670020http://purl.uniprot.org/core/author"Miyazono K."xsd:string
http://purl.uniprot.org/citations/9670020http://purl.uniprot.org/core/author"Kawabata M."xsd:string
http://purl.uniprot.org/citations/9670020http://purl.uniprot.org/core/author"Kawabata M."xsd:string
http://purl.uniprot.org/citations/9670020http://purl.uniprot.org/core/author"Hanyu A."xsd:string
http://purl.uniprot.org/citations/9670020http://purl.uniprot.org/core/author"Hanyu A."xsd:string
http://purl.uniprot.org/citations/9670020http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9670020http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9670020http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/9670020http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/9670020http://purl.uniprot.org/core/pages"4056-4065"xsd:string
http://purl.uniprot.org/citations/9670020http://purl.uniprot.org/core/pages"4056-4065"xsd:string
http://purl.uniprot.org/citations/9670020http://purl.uniprot.org/core/title"Smad proteins exist as monomers in vivo and undergo homo- and hetero-oligomerization upon activation by serine/threonine kinase receptors."xsd:string
http://purl.uniprot.org/citations/9670020http://purl.uniprot.org/core/title"Smad proteins exist as monomers in vivo and undergo homo- and hetero-oligomerization upon activation by serine/threonine kinase receptors."xsd:string
http://purl.uniprot.org/citations/9670020http://purl.uniprot.org/core/volume"17"xsd:string
http://purl.uniprot.org/citations/9670020http://purl.uniprot.org/core/volume"17"xsd:string