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http://purl.uniprot.org/citations/25100727http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/25100727http://www.w3.org/2000/01/rdf-schema#comment"The bone morphogenetic protein (BMP) signaling pathway regulates a wide range of cellular responses in metazoans. A key step in the canonical BMP signaling is the phosphorylation and activation of transcription factors Smad1, Smad5, and Smad8 (collectively Smad1/5/8) by the type I BMP receptors. We previously identified PPM1A as a phosphatase toward dephosphorylation of all receptor-regulated Smads (R-Smads), including Smad1/5/8. Here we report another nuclear phosphatase named SCP4/CTDSPL2, belonging to the FCP/SCP family, as a novel Smad phosphatase in the nucleus. SCP4 physically interacts with and specifically dephosphorylates Smad1/5/8, and as a result attenuates BMP-induced transcriptional responses. Knockdown of SCP4 in multipotent mesenchymal C2C12 cells leads to increased expression of BMP target genes and consequently promotes BMP-induced osteogenic differentiation. Collectively, our results demonstrate that SCP4, as a Smad phosphatase, plays a critical role in BMP-induced signaling and cellular functions."xsd:string
http://purl.uniprot.org/citations/25100727http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m114.568964"xsd:string
http://purl.uniprot.org/citations/25100727http://purl.uniprot.org/core/author"Lin X."xsd:string
http://purl.uniprot.org/citations/25100727http://purl.uniprot.org/core/author"Sun B."xsd:string
http://purl.uniprot.org/citations/25100727http://purl.uniprot.org/core/author"Zhang Z."xsd:string
http://purl.uniprot.org/citations/25100727http://purl.uniprot.org/core/author"Zhao Y."xsd:string
http://purl.uniprot.org/citations/25100727http://purl.uniprot.org/core/author"Xiao M."xsd:string
http://purl.uniprot.org/citations/25100727http://purl.uniprot.org/core/author"Duan X."xsd:string
http://purl.uniprot.org/citations/25100727http://purl.uniprot.org/core/author"Feng X.H."xsd:string
http://purl.uniprot.org/citations/25100727http://purl.uniprot.org/core/author"Yu P.B."xsd:string
http://purl.uniprot.org/citations/25100727http://purl.uniprot.org/core/author"Shen T."xsd:string
http://purl.uniprot.org/citations/25100727http://purl.uniprot.org/core/date"2014"xsd:gYear
http://purl.uniprot.org/citations/25100727http://purl.uniprot.org/core/name"J Biol Chem"xsd:string
http://purl.uniprot.org/citations/25100727http://purl.uniprot.org/core/pages"26441-26450"xsd:string
http://purl.uniprot.org/citations/25100727http://purl.uniprot.org/core/title"C-terminal domain (CTD) small phosphatase-like 2 modulates the canonical bone morphogenetic protein (BMP) signaling and mesenchymal differentiation via Smad dephosphorylation."xsd:string
http://purl.uniprot.org/citations/25100727http://purl.uniprot.org/core/volume"289"xsd:string
http://purl.uniprot.org/citations/25100727http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/25100727
http://purl.uniprot.org/citations/25100727http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/25100727
http://purl.uniprot.org/uniprot/Q8BG15#attribution-BD0DF476C3B5E316921E49DB6D4532E2http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/25100727
http://purl.uniprot.org/uniprot/Q8BG15#attribution-C9C64F375DB9C07BC18BB3630C79E19Fhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/25100727
http://purl.uniprot.org/uniprot/P49443#attribution-BD0DF476C3B5E316921E49DB6D4532E2http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/25100727
http://purl.uniprot.org/uniprot/P49443#attribution-C9C64F375DB9C07BC18BB3630C79E19Fhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/25100727
http://purl.uniprot.org/uniprot/P70340#attribution-C9C64F375DB9C07BC18BB3630C79E19Fhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/25100727
http://purl.uniprot.org/uniprot/#_A0A1Y7VJZ4-mappedCitation-25100727http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/25100727