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10.18632/oncotarget.9914 http://scihub22266oqcxt.onion/10.18632/oncotarget.9914 C5342353!5342353 !27303920     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=27303920 &cmd=llinks): Failed to open stream: HTTP request failed! 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Scaffold attachment factor A (SAF-A) and Ku temporally regulate repair of radiation-induced clustered genome lesions |pdf=|usr=}}{{27303920 }} gab.com Text Scaffold attachment factor A (SAF-A) and Ku temporally regulate repair of radiation-induced clustered genome lesions JO: Oncotarget http://www.kidney.de/pget.php?&tw=1&pmid=27303920 #FOAvip Ionizing radiation (IR) induces highly cytotoxic double-strand breaks (DSBs) and also clustered oxidized bases in mammalian genomes. Base excision repair (BER) of bi-stranded oxidized bases could generate additional DSBs as repair intermediates in the vicinity of direct DSBs, leading to loss of DNA fragments. This could be avoided if DSB repair via DNA-PK-mediated nonhomologous end joining (NHEJ) precedes BER initiated by NEIL1 and other DNA glycosylases (DGs). Here we show that DNA-PK subunit Ku inhibits DGs via direct interaction. The scaffold attachment factor (SAF)-A, (also called hnRNP-U), phosphorylated at Ser59 by DNA-PK early after IR treatment, is linked to transient release of chromatin-bound NEIL1, thus preventing BER. SAF-A is subsequently dephosphorylated. Ku inhibition of DGs in vitro is relieved by unphosphorylated SAF-A, but not by the phosphomimetic Asp59 mutant. We thus propose that SAF-A, in concert with Ku, temporally regulates base damage repair in irradiated cell genome. Twit Text FOAVip Scaffold attachment factor A (SAF-A) and Ku temporally regulate repair of radiation-induced clustered genome lesions ????Oncotarget http://www.kidney.de/pget.php?&tw=1&pmid=27303920 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27303920 #FOAvip English Wikipedia <ref>{{Cite pmid|27303920 }}</ref> Scaffold attachment factor A (SAF-A) and Ku temporally regulate repair of radiation-induced clustered genome lesions #MMPMID27303920 Hegde ML ; Dutta A ; Yang C ; Mantha AK ; Hegde PM ; Pandey A ; Sengupta S ; Yu Y ; Calsou P ; Chen D ; Lees-Miller SP ; Mitra S Oncotarget 2016[Aug]; 7 (34 ): 54430-54444 PMID27303920 show ga Ionizing radiation (IR) induces highly cytotoxic double-strand breaks (DSBs) and also clustered oxidized bases in mammalian genomes. Base excision repair (BER) of bi-stranded oxidized bases could generate additional DSBs as repair intermediates in the vicinity of direct DSBs, leading to loss of DNA fragments. This could be avoided if DSB repair via DNA-PK-mediated nonhomologous end joining (NHEJ) precedes BER initiated by NEIL1 and other DNA glycosylases (DGs). Here we show that DNA-PK subunit Ku inhibits DGs via direct interaction. The scaffold attachment factor (SAF)-A, (also called hnRNP-U), phosphorylated at Ser59 by DNA-PK early after IR treatment, is linked to transient release of chromatin-bound NEIL1, thus preventing BER. SAF-A is subsequently dephosphorylated. Ku inhibition of DGs in vitro is relieved by unphosphorylated SAF-A, but not by the phosphomimetic Asp59 mutant. We thus propose that SAF-A, in concert with Ku, temporally regulates base damage repair in irradiated cell genome. |*DNA Repair [MESH] |DNA Breaks, Double-Stranded [MESH] |DNA Glycosylases/physiology [MESH] |DNA Repair Enzymes/physiology [MESH] |DNA-(Apurinic or Apyrimidinic Site) Lyase/physiology [MESH] |DNA-Activated Protein Kinase/physiology [MESH] |DNA-Binding Proteins/physiology [MESH] |HEK293 Cells [MESH] |Heterogeneous-Nuclear Ribonucleoprotein U/*physiology [MESH] |Humans [MESH] |Ku Autoantigen/*physiology [MESH] |Phosphorylation [MESH] |Radiation Injuries/*etiology [MESH]Scaffold attachment factor A (SAF-A) and Ku temporally regulate repair(epmc).pdf DeepDyve Pubget Overpricing