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http://purl.uniprot.org/citations/30154440http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/30154440http://www.w3.org/2000/01/rdf-schema#comment"Trimethylation of histone H3 on lysine-4 (H3K4me3) is associated with gene-regulatory elements, but its transcription-independent function in cell division is unclear. CxxC-finger protein-1 (CFP1) is a major mediator of H3K4 trimethylation in mouse oocytes. Here we report that oocyte-specific knockout of Cxxc1, inhibition of CFP1 function, or abrogation of H3K4 methylation in oocytes each causes a delay of meiotic resumption as well as metaphase I arrest owing to defective spindle assembly and chromosome misalignment. These phenomena are partially attributed to insufficient phosphorylation of histone H3 at threonine-3. CDK1 triggers cell division-coupled degradation and inhibitory phosphorylation of CFP1. Preventing CFP1 degradation and phosphorylation causes CFP1 accumulation on chromosomes and impairs meiotic maturation and preimplantation embryo development. Therefore, CFP1-mediated H3K4 trimethylation provides 3a permission signal for the G2-M transition. Dual inhibition of CFP1 removes the SETD1-CFP1 complex from chromatin and ensures appropriate chromosome configuration changes during meiosis and mitosis."xsd:string
http://purl.uniprot.org/citations/30154440http://purl.org/dc/terms/identifier"doi:10.1038/s41467-018-05930-x"xsd:string
http://purl.uniprot.org/citations/30154440http://purl.uniprot.org/core/author"Jiang Y."xsd:string
http://purl.uniprot.org/citations/30154440http://purl.uniprot.org/core/author"Liu J."xsd:string
http://purl.uniprot.org/citations/30154440http://purl.uniprot.org/core/author"Yu C."xsd:string
http://purl.uniprot.org/citations/30154440http://purl.uniprot.org/core/author"Zhang S.Y."xsd:string
http://purl.uniprot.org/citations/30154440http://purl.uniprot.org/core/author"Jiang J.C."xsd:string
http://purl.uniprot.org/citations/30154440http://purl.uniprot.org/core/author"Dai X.X."xsd:string
http://purl.uniprot.org/citations/30154440http://purl.uniprot.org/core/author"Fan H.Y."xsd:string
http://purl.uniprot.org/citations/30154440http://purl.uniprot.org/core/author"Sha Q.Q."xsd:string
http://purl.uniprot.org/citations/30154440http://purl.uniprot.org/core/author"Ou X.H."xsd:string
http://purl.uniprot.org/citations/30154440http://purl.uniprot.org/core/date"2018"xsd:gYear
http://purl.uniprot.org/citations/30154440http://purl.uniprot.org/core/name"Nat Commun"xsd:string
http://purl.uniprot.org/citations/30154440http://purl.uniprot.org/core/pages"3477"xsd:string
http://purl.uniprot.org/citations/30154440http://purl.uniprot.org/core/title"CFP1 coordinates histone H3 lysine-4 trimethylation and meiotic cell cycle progression in mouse oocytes."xsd:string
http://purl.uniprot.org/citations/30154440http://purl.uniprot.org/core/volume"9"xsd:string
http://purl.uniprot.org/citations/30154440http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/30154440
http://purl.uniprot.org/citations/30154440http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/30154440
http://purl.uniprot.org/uniprot/#_Q3UIZ4-mappedCitation-30154440http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/30154440
http://purl.uniprot.org/uniprot/#_P11440-mappedCitation-30154440http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/30154440
http://purl.uniprot.org/uniprot/#_Q541B1-mappedCitation-30154440http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/30154440
http://purl.uniprot.org/uniprot/#_Q9CWW7-mappedCitation-30154440http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/30154440
http://purl.uniprot.org/uniprot/P11440http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/30154440
http://purl.uniprot.org/uniprot/Q541B1http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/30154440