Global γH2AX phosphorylation in Drosophila is reversed by the phosphatase Mts

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).

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Journal
PubMed
Published
2024-12-18
DOI
https://doi.org/10.17912/micropub.biology.001474
Citations
1
Primary Topic
Enzyme Structure and Function
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article
Field-Weighted Citation Impact
0.12
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article

Global γH2AX phosphorylation in Drosophila is reversed by the phosphatase Mts

Peter B. Becker, Zivkos Apostolou, Silke Krause
1 citations
PubMed
Enzyme Structure and Function
0.12
article

Global γH2AX phosphorylation in Drosophila is reversed by the phosphatase Mts

Peter B. Becker, Zivkos Apostolou, Silke Krause
article en
1 citations

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 <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).

PubMedVol. 2025
Ludwig-Maximilians-Universität München (DE)
Openalex Percentile: Top 56%
Enzyme Structure and Function
0.12
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