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http://purl.uniprot.org/citations/28122957http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/28122957http://www.w3.org/2000/01/rdf-schema#comment"Glycolytic enzymes are known to play pivotal roles in cancer cell survival, yet their molecular mechanisms remain poorly understood. Phosphoglycerate mutase 1 (PGAM1) is an important glycolytic enzyme that coordinates glycolysis, pentose phosphate pathway, and serine biosynthesis in cancer cells. Herein, we report that PGAM1 is required for homologous recombination (HR) repair of DNA double-strand breaks (DSBs) caused by DNA-damaging agents. Mechanistically, PGAM1 facilitates DSB end resection by regulating the stability of CTBP-interacting protein (CtIP). Knockdown of PGAM1 in cancer cells accelerates CtIP degradation through deprivation of the intracellular deoxyribonucleotide triphosphate pool and associated activation of the p53/p73 pathway. Enzymatic inhibition of PGAM1 decreases CtIP protein levels, impairs HR repair, and hence sensitizes BRCA1/2-proficient breast cancer to poly(ADP-ribose) polymerase (PARP) inhibitors. Together, this study identifies a metabolically dependent function of PGAM1 in promoting HR repair and reveals a potential therapeutic opportunity for PGAM1 inhibitors in combination with PARP inhibitors."xsd:string
http://purl.uniprot.org/citations/28122957http://purl.org/dc/terms/identifier"doi:10.1083/jcb.201607008"xsd:string
http://purl.uniprot.org/citations/28122957http://purl.uniprot.org/core/author"Ding J."xsd:string
http://purl.uniprot.org/citations/28122957http://purl.uniprot.org/core/author"Lv H."xsd:string
http://purl.uniprot.org/citations/28122957http://purl.uniprot.org/core/author"Sun W."xsd:string
http://purl.uniprot.org/citations/28122957http://purl.uniprot.org/core/author"Tan M."xsd:string
http://purl.uniprot.org/citations/28122957http://purl.uniprot.org/core/author"Xu J."xsd:string
http://purl.uniprot.org/citations/28122957http://purl.uniprot.org/core/author"Xie Z."xsd:string
http://purl.uniprot.org/citations/28122957http://purl.uniprot.org/core/author"Zhong J."xsd:string
http://purl.uniprot.org/citations/28122957http://purl.uniprot.org/core/author"Qu J."xsd:string
http://purl.uniprot.org/citations/28122957http://purl.uniprot.org/core/author"Zhu M."xsd:string
http://purl.uniprot.org/citations/28122957http://purl.uniprot.org/core/author"Huang M."xsd:string
http://purl.uniprot.org/citations/28122957http://purl.uniprot.org/core/author"Jin N."xsd:string
http://purl.uniprot.org/citations/28122957http://purl.uniprot.org/core/author"Geng M."xsd:string
http://purl.uniprot.org/citations/28122957http://purl.uniprot.org/core/author"Lin S.H."xsd:string
http://purl.uniprot.org/citations/28122957http://purl.uniprot.org/core/date"2017"xsd:gYear
http://purl.uniprot.org/citations/28122957http://purl.uniprot.org/core/name"J Cell Biol"xsd:string
http://purl.uniprot.org/citations/28122957http://purl.uniprot.org/core/pages"409-424"xsd:string
http://purl.uniprot.org/citations/28122957http://purl.uniprot.org/core/title"Phosphoglycerate mutase 1 regulates dNTP pool and promotes homologous recombination repair in cancer cells."xsd:string
http://purl.uniprot.org/citations/28122957http://purl.uniprot.org/core/volume"216"xsd:string
http://purl.uniprot.org/citations/28122957http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/28122957
http://purl.uniprot.org/citations/28122957http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/28122957
http://purl.uniprot.org/uniprot/#_B4DKL5-mappedCitation-28122957http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/28122957
http://purl.uniprot.org/uniprot/#_B4DMJ7-mappedCitation-28122957http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/28122957