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http://purl.uniprot.org/citations/9136927http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9136927http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9136927http://www.w3.org/2000/01/rdf-schema#comment"Bone morphogenetic proteins (BMPs) are members of the TGF-beta family that regulate cell proliferation, apoptosis, and differentiation, and participate in the development of most tissues and organs in vertebrates. Smad proteins function downstream of TGF-beta receptor serine/threonine kinases and undergo serine phosphorylation in response to receptor activation. Smad1 is regulated in this fashion by BMP receptors, and Smad2 and Smad3 by TGF-beta and activin receptors. Here, we report that BMP receptors phosphorylate and activate Smad1 directly. Phosphorylation of Smad1 in vivo involves serines in the carboxy-terminal motif SSXS. These residues are phosphorylated directly by a BMP type I receptor in vitro. Mutation of these carboxy-terminal serines prevents several Smad1 activation events, namely, Smad1 association with the related protein DPC4, accumulation in the nucleus, and gain of transcriptional activity. Similar carboxy-terminal serines in Smad2 are required for its phosphorylation and association with DPC4 in response to TGF-beta, indicating the generality of this process of Smad activation. As a direct physiological substrate of BMP receptors, Smad1 provides a link between receptor serine/threonine kinases and the nucleus."xsd:string
http://purl.uniprot.org/citations/9136927http://purl.org/dc/terms/identifier"doi:10.1101/gad.11.8.984"xsd:string
http://purl.uniprot.org/citations/9136927http://purl.org/dc/terms/identifier"doi:10.1101/gad.11.8.984"xsd:string
http://purl.uniprot.org/citations/9136927http://purl.uniprot.org/core/author"Liu F."xsd:string
http://purl.uniprot.org/citations/9136927http://purl.uniprot.org/core/author"Liu F."xsd:string
http://purl.uniprot.org/citations/9136927http://purl.uniprot.org/core/author"Massague J."xsd:string
http://purl.uniprot.org/citations/9136927http://purl.uniprot.org/core/author"Massague J."xsd:string
http://purl.uniprot.org/citations/9136927http://purl.uniprot.org/core/author"Hata A."xsd:string
http://purl.uniprot.org/citations/9136927http://purl.uniprot.org/core/author"Hata A."xsd:string
http://purl.uniprot.org/citations/9136927http://purl.uniprot.org/core/author"Doody J."xsd:string
http://purl.uniprot.org/citations/9136927http://purl.uniprot.org/core/author"Doody J."xsd:string
http://purl.uniprot.org/citations/9136927http://purl.uniprot.org/core/author"Kretzschmar M."xsd:string
http://purl.uniprot.org/citations/9136927http://purl.uniprot.org/core/author"Kretzschmar M."xsd:string
http://purl.uniprot.org/citations/9136927http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9136927http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9136927http://purl.uniprot.org/core/name"Genes Dev."xsd:string
http://purl.uniprot.org/citations/9136927http://purl.uniprot.org/core/name"Genes Dev."xsd:string
http://purl.uniprot.org/citations/9136927http://purl.uniprot.org/core/pages"984-995"xsd:string
http://purl.uniprot.org/citations/9136927http://purl.uniprot.org/core/pages"984-995"xsd:string
http://purl.uniprot.org/citations/9136927http://purl.uniprot.org/core/title"The TGF-beta family mediator Smad1 is phosphorylated directly and activated functionally by the BMP receptor kinase."xsd:string
http://purl.uniprot.org/citations/9136927http://purl.uniprot.org/core/title"The TGF-beta family mediator Smad1 is phosphorylated directly and activated functionally by the BMP receptor kinase."xsd:string
http://purl.uniprot.org/citations/9136927http://purl.uniprot.org/core/volume"11"xsd:string
http://purl.uniprot.org/citations/9136927http://purl.uniprot.org/core/volume"11"xsd:string