PubMed:21330363 JSONTXT

{"project":"sentences","denotations":[{"id":"T1","span":{"begin":0,"end":93},"obj":"Sentence"},{"id":"T2","span":{"begin":94,"end":293},"obj":"Sentence"},{"id":"T3","span":{"begin":294,"end":444},"obj":"Sentence"},{"id":"T4","span":{"begin":445,"end":600},"obj":"Sentence"},{"id":"T5","span":{"begin":601,"end":728},"obj":"Sentence"},{"id":"T6","span":{"begin":729,"end":899},"obj":"Sentence"},{"id":"T7","span":{"begin":900,"end":1100},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Involvement of DNA-dependent protein kinase in normal cell cycle progression through mitosis.\nThe catalytic subunit of DNA-dependent protein kinase (DNA-PKcs) plays an important role in DNA double-strand break (DSB) repair as the underlying mechanism of the non-homologous end joining pathway. When DSBs occur, DNA-PKcs is rapidly phosphorylated at both the Thr-2609 and Ser-2056 residues, and such phosphorylations are critical for DSB repair. In this study we report that, in addition to responding to DSBs, DNA-PKcs is activated and phosphorylated in normal cell cycle progression through mitosis. Mitotic induction of DNA-PKcs phosphorylation is closely associated with the spindle apparatus at centrosomes and kinetochores. Furthermore, depletion of DNA-PKcs protein levels or inhibition of DNA-PKcs kinase activity results in the delay of mitotic transition because of chromosome misalignment. These results demonstrate for the first time that DNA-PKcs, in addition to its role in DSB repair, is a critical regulator of mitosis and could modulate microtubule dynamics in chromosome segregation."}

{"project":"Allie","denotations":[{"id":"SS1_21330363_1_0","span":{"begin":190,"end":209},"obj":"expanded"},{"id":"SS2_21330363_1_0","span":{"begin":211,"end":214},"obj":"abbr"}],"relations":[{"id":"AE1_21330363_1_0","pred":"abbreviatedTo","subj":"SS1_21330363_1_0","obj":"SS2_21330363_1_0"}],"text":"Involvement of DNA-dependent protein kinase in normal cell cycle progression through mitosis.\nThe catalytic subunit of DNA-dependent protein kinase (DNA-PKcs) plays an important role in DNA double-strand break (DSB) repair as the underlying mechanism of the non-homologous end joining pathway. When DSBs occur, DNA-PKcs is rapidly phosphorylated at both the Thr-2609 and Ser-2056 residues, and such phosphorylations are critical for DSB repair. In this study we report that, in addition to responding to DSBs, DNA-PKcs is activated and phosphorylated in normal cell cycle progression through mitosis. Mitotic induction of DNA-PKcs phosphorylation is closely associated with the spindle apparatus at centrosomes and kinetochores. Furthermore, depletion of DNA-PKcs protein levels or inhibition of DNA-PKcs kinase activity results in the delay of mitotic transition because of chromosome misalignment. These results demonstrate for the first time that DNA-PKcs, in addition to its role in DSB repair, is a critical regulator of mitosis and could modulate microtubule dynamics in chromosome segregation."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":54,"end":64},"obj":"Body_part"},{"id":"T2","span":{"begin":561,"end":571},"obj":"Body_part"},{"id":"T3","span":{"begin":875,"end":885},"obj":"Body_part"},{"id":"T4","span":{"begin":1053,"end":1064},"obj":"Body_part"},{"id":"T5","span":{"begin":1077,"end":1087},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_2000098"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_2000098"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/GO_0005694"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/GO_0005874"},{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/GO_0005694"}],"text":"Involvement of DNA-dependent protein kinase in normal cell cycle progression through mitosis.\nThe catalytic subunit of DNA-dependent protein kinase (DNA-PKcs) plays an important role in DNA double-strand break (DSB) repair as the underlying mechanism of the non-homologous end joining pathway. When DSBs occur, DNA-PKcs is rapidly phosphorylated at both the Thr-2609 and Ser-2056 residues, and such phosphorylations are critical for DSB repair. In this study we report that, in addition to responding to DSBs, DNA-PKcs is activated and phosphorylated in normal cell cycle progression through mitosis. Mitotic induction of DNA-PKcs phosphorylation is closely associated with the spindle apparatus at centrosomes and kinetochores. Furthermore, depletion of DNA-PKcs protein levels or inhibition of DNA-PKcs kinase activity results in the delay of mitotic transition because of chromosome misalignment. These results demonstrate for the first time that DNA-PKcs, in addition to its role in DSB repair, is a critical regulator of mitosis and could modulate microtubule dynamics in chromosome segregation."}