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http://purl.uniprot.org/citations/34936881http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/34936881http://www.w3.org/2000/01/rdf-schema#comment"The DNA-dependent protein kinase (DNA-PK) initially protects broken DNA ends but then promotes their processing during non-homologous end joining (NHEJ). Before ligation by NHEJ, DNA hairpin ends generated during V(D)J recombination must be opened by the Artemis nuclease, together with autophosphorylated DNA-PK. Structures of DNA-PK bound to DNA before and after phosphorylation, and in complex with Artemis and a DNA hairpin, reveal an essential functional switch. When bound to open DNA ends in its protection mode, DNA-PK is inhibited for cis-autophosphorylation of the so-called ABCDE cluster but activated for phosphorylation of other targets. In contrast, DNA hairpin ends promote cis-autophosphorylation. Phosphorylation of four Thr residues in ABCDE leads to gross structural rearrangement of DNA-PK, widening the DNA binding groove for Artemis recruitment and hairpin cleavage. Meanwhile, Artemis locks DNA-PK into the kinase-inactive state. Kinase activity and autophosphorylation of DNA-PK are regulated by different DNA ends, feeding forward to coordinate NHEJ events."xsd:string
http://purl.uniprot.org/citations/34936881http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2021.11.025"xsd:string
http://purl.uniprot.org/citations/34936881http://purl.uniprot.org/core/author"Chen X."xsd:string
http://purl.uniprot.org/citations/34936881http://purl.uniprot.org/core/author"Li J."xsd:string
http://purl.uniprot.org/citations/34936881http://purl.uniprot.org/core/author"Liu L."xsd:string
http://purl.uniprot.org/citations/34936881http://purl.uniprot.org/core/author"Wang H."xsd:string
http://purl.uniprot.org/citations/34936881http://purl.uniprot.org/core/author"Yang W."xsd:string
http://purl.uniprot.org/citations/34936881http://purl.uniprot.org/core/author"Gellert M."xsd:string
http://purl.uniprot.org/citations/34936881http://purl.uniprot.org/core/author"Meek K."xsd:string
http://purl.uniprot.org/citations/34936881http://purl.uniprot.org/core/author"Buehl C.J."xsd:string
http://purl.uniprot.org/citations/34936881http://purl.uniprot.org/core/author"Goff N.J."xsd:string
http://purl.uniprot.org/citations/34936881http://purl.uniprot.org/core/date"2022"xsd:gYear
http://purl.uniprot.org/citations/34936881http://purl.uniprot.org/core/name"Mol Cell"xsd:string
http://purl.uniprot.org/citations/34936881http://purl.uniprot.org/core/pages"177-189.e4"xsd:string
http://purl.uniprot.org/citations/34936881http://purl.uniprot.org/core/title"Autophosphorylation transforms DNA-PK from protecting to processing DNA ends."xsd:string
http://purl.uniprot.org/citations/34936881http://purl.uniprot.org/core/volume"82"xsd:string
http://purl.uniprot.org/citations/34936881http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/34936881
http://purl.uniprot.org/citations/34936881http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/34936881
http://purl.uniprot.org/uniprot/#_B4DL41-mappedCitation-34936881http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/34936881
http://purl.uniprot.org/uniprot/#_P78527-mappedCitation-34936881http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/34936881
http://purl.uniprot.org/uniprot/#_P12956-mappedCitation-34936881http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/34936881
http://purl.uniprot.org/uniprot/#_P13010-mappedCitation-34936881http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/34936881
http://purl.uniprot.org/uniprot/#_Q96SD1-mappedCitation-34936881http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/34936881
http://purl.uniprot.org/uniprot/P12956http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/34936881