{"title":"Global γH2AX phosphorylation in <i>Drosophila</i> is reversed by the phosphatase Mts.","authors":"Zivkos Apostolou, Silke Krause, Peter B Becker","doi":"10.17912/micropub.biology.001474","DOIUrl":null,"url":null,"abstract":"<p><p>The phosphorylation of the histone variant H2AX to form γH2AX is an early and critical histone modification during the DNA damage response. This phosphorylation has proven to be a highly specific molecular marker for tracking the initiation and resolution of DNA damage. In this study, we investigate the roles of three phosphatases in removing the 'γ' phospho-epitope from H2AX in <i>Drosophila</i> Kc167 cells. We found that the bulk of the X-ray-induced γH2AX signal is erased by the PP2A-type phosphatase MTS (microtubule star).</p>","PeriodicalId":74192,"journal":{"name":"microPublication biology","volume":"2025 ","pages":""},"PeriodicalIF":0.0000,"publicationDate":"2025-02-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11883472/pdf/","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"microPublication biology","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.17912/micropub.biology.001474","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2025/1/1 0:00:00","PubModel":"eCollection","JCR":"","JCRName":"","Score":null,"Total":0}
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Abstract
The phosphorylation of the histone variant H2AX to form γH2AX is an early and critical histone modification during the DNA damage response. This phosphorylation has proven to be a highly specific molecular marker for tracking the initiation and resolution of DNA damage. In this study, we investigate the roles of three phosphatases in removing the 'γ' phospho-epitope from H2AX in Drosophila Kc167 cells. We found that the bulk of the X-ray-induced γH2AX signal is erased by the PP2A-type phosphatase MTS (microtubule star).
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