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http://purl.uniprot.org/citations/17981124http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17981124http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17981124http://www.w3.org/2000/01/rdf-schema#comment"SUMOylation is a dynamic process, catalyzed by SUMO-specific ligases and reversed by Sentrin/SUMO-specific proteases (SENPs). The physiologic consequences of SUMOylation and deSUMOylation are not fully understood. Here we investigate the phenotypes of mice lacking SENP1 and find that SENP1(-/-) embryos show severe fetal anemia stemming from deficient erythropoietin (Epo) production and die midgestation. We determine that SENP1 controls Epo production by regulating the stability of hypoxia-inducible factor 1alpha (HIF1alpha) during hypoxia. Hypoxia induces SUMOylation of HIF1alpha, which promotes its binding to a ubiquitin ligase, von Hippel-Lindau (VHL) protein, through a proline hydroxylation-independent mechanism, leading to its ubiquitination and degradation. In SENP1(-/-) MEFs, hypoxia-induced transcription of HIF1alpha-dependent genes such as vascular endothelial growth factor (VEGF) and glucose transporter 1 (Glut-1) is markedly reduced. These results show that SENP1 plays a key role in the regulation of the hypoxic response through regulation of HIF1alpha stability and that SUMOylation can serve as a direct signal for ubiquitin-dependent degradation."xsd:string
http://purl.uniprot.org/citations/17981124http://purl.org/dc/terms/identifier"doi:10.1016/j.cell.2007.08.045"xsd:string
http://purl.uniprot.org/citations/17981124http://purl.org/dc/terms/identifier"doi:10.1016/j.cell.2007.08.045"xsd:string
http://purl.uniprot.org/citations/17981124http://purl.uniprot.org/core/author"Cheng J."xsd:string
http://purl.uniprot.org/citations/17981124http://purl.uniprot.org/core/author"Cheng J."xsd:string
http://purl.uniprot.org/citations/17981124http://purl.uniprot.org/core/author"Zhang S."xsd:string
http://purl.uniprot.org/citations/17981124http://purl.uniprot.org/core/author"Zhang S."xsd:string
http://purl.uniprot.org/citations/17981124http://purl.uniprot.org/core/author"Kang X."xsd:string
http://purl.uniprot.org/citations/17981124http://purl.uniprot.org/core/author"Kang X."xsd:string
http://purl.uniprot.org/citations/17981124http://purl.uniprot.org/core/author"Yeh E.T.H."xsd:string
http://purl.uniprot.org/citations/17981124http://purl.uniprot.org/core/author"Yeh E.T.H."xsd:string
http://purl.uniprot.org/citations/17981124http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17981124http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17981124http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/17981124http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/17981124http://purl.uniprot.org/core/pages"584-595"xsd:string
http://purl.uniprot.org/citations/17981124http://purl.uniprot.org/core/pages"584-595"xsd:string
http://purl.uniprot.org/citations/17981124http://purl.uniprot.org/core/title"SUMO-specific protease 1 is essential for stabilization of HIF1alpha during hypoxia."xsd:string
http://purl.uniprot.org/citations/17981124http://purl.uniprot.org/core/title"SUMO-specific protease 1 is essential for stabilization of HIF1alpha during hypoxia."xsd:string
http://purl.uniprot.org/citations/17981124http://purl.uniprot.org/core/volume"131"xsd:string
http://purl.uniprot.org/citations/17981124http://purl.uniprot.org/core/volume"131"xsd:string
http://purl.uniprot.org/citations/17981124http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17981124
http://purl.uniprot.org/citations/17981124http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17981124