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http://purl.uniprot.org/citations/25547115http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/25547115http://www.w3.org/2000/01/rdf-schema#comment"PTEN [phosphatidylinositol (3,4,5)-trisphosphate phosphatase and tensin homolog deleted from chromosome 10], a phosphatase and critical tumor suppressor, is regulated by numerous post-translational modifications, including phosphorylation, ubiquitination, acetylation, and SUMOylation, which affect PTEN localization and protein stability. Here we report ADP-ribosylation as a new post-translational modification of PTEN. We identified PTEN as a novel substrate of tankyrases, which are members of the poly(ADP-ribose) polymerases (PARPs). We showed that tankyrases interact with and ribosylate PTEN, which promotes the recognition of PTEN by a PAR-binding E3 ubiquitin ligase, RNF146, leading to PTEN ubiquitination and degradation. Double knockdown of tankyrase1/2 stabilized PTEN, resulting in the subsequent down-regulation of AKT phosphorylation and thus suppressed cell proliferation and glycolysis in vitro and tumor growth in vivo. Furthermore, tankyrases were up-regulated and negatively correlated with PTEN expression in human colon carcinomas. Together, our study revealed a new regulation of PTEN and highlighted a role for tankyrases in the PTEN-AKT pathway that can be explored further for cancer treatment."xsd:string
http://purl.uniprot.org/citations/25547115http://purl.org/dc/terms/identifier"doi:10.1101/gad.251785.114"xsd:string
http://purl.uniprot.org/citations/25547115http://purl.uniprot.org/core/author"Chen J."xsd:string
http://purl.uniprot.org/citations/25547115http://purl.uniprot.org/core/author"Feng L."xsd:string
http://purl.uniprot.org/citations/25547115http://purl.uniprot.org/core/author"Han X."xsd:string
http://purl.uniprot.org/citations/25547115http://purl.uniprot.org/core/author"Li N."xsd:string
http://purl.uniprot.org/citations/25547115http://purl.uniprot.org/core/author"Liang K."xsd:string
http://purl.uniprot.org/citations/25547115http://purl.uniprot.org/core/author"Lin C."xsd:string
http://purl.uniprot.org/citations/25547115http://purl.uniprot.org/core/author"Zhang Y."xsd:string
http://purl.uniprot.org/citations/25547115http://purl.uniprot.org/core/author"Wang J."xsd:string
http://purl.uniprot.org/citations/25547115http://purl.uniprot.org/core/author"Yang L."xsd:string
http://purl.uniprot.org/citations/25547115http://purl.uniprot.org/core/author"Yu Y."xsd:string
http://purl.uniprot.org/citations/25547115http://purl.uniprot.org/core/author"Wang W."xsd:string
http://purl.uniprot.org/citations/25547115http://purl.uniprot.org/core/author"Songyang Z."xsd:string
http://purl.uniprot.org/citations/25547115http://purl.uniprot.org/core/date"2015"xsd:gYear
http://purl.uniprot.org/citations/25547115http://purl.uniprot.org/core/name"Genes Dev"xsd:string
http://purl.uniprot.org/citations/25547115http://purl.uniprot.org/core/pages"157-170"xsd:string
http://purl.uniprot.org/citations/25547115http://purl.uniprot.org/core/title"Poly-ADP ribosylation of PTEN by tankyrases promotes PTEN degradation and tumor growth."xsd:string
http://purl.uniprot.org/citations/25547115http://purl.uniprot.org/core/volume"29"xsd:string
http://purl.uniprot.org/citations/25547115http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/25547115
http://purl.uniprot.org/citations/25547115http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/25547115
http://purl.uniprot.org/uniprot/#_Q15008-mappedCitation-25547115http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/25547115
http://purl.uniprot.org/uniprot/#_A5LHX3-mappedCitation-25547115http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/25547115
http://purl.uniprot.org/uniprot/#_O43242-mappedCitation-25547115http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/25547115