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Tyrosine dephosphorylation of H2AX modulates apoptosis and survival decisions

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  • Peter J. Cook

    (Howard Hughes Medical Institute School of Medicine, University of California, San Diego, California 92037, USA
    School of Medicine, University of California, San Diego, California 92093, USA)

  • Bong Gun Ju

    (Howard Hughes Medical Institute School of Medicine, University of California, San Diego, California 92037, USA
    Sogang University)

  • Francesca Telese

    (Howard Hughes Medical Institute School of Medicine, University of California, San Diego, California 92037, USA)

  • Xiangting Wang

    (Howard Hughes Medical Institute School of Medicine, University of California, San Diego, California 92037, USA)

  • Christopher K. Glass

    (School of Medicine, University of California, San Diego, 9500 Gilman Drive, La Jolla, California 92093, USA)

  • Michael G. Rosenfeld

    (Howard Hughes Medical Institute School of Medicine, University of California, San Diego, California 92037, USA)

Abstract

Life and death fate decisions allow cells to avoid massive apoptotic death in response to genotoxic stress. Although the regulatory mechanisms and signalling pathways controlling DNA repair and apoptosis are well characterized, the precise molecular strategies that determine the ultimate choice of DNA repair and survival or apoptotic cell death remain incompletely understood. Here we report that a protein tyrosine phosphatase, EYA, is involved in promoting efficient DNA repair rather than apoptosis in response to genotoxic stress in mammalian embryonic kidney cells by executing a damage-signal-dependent dephosphorylation of an H2AX carboxy-terminal tyrosine phosphate (Y142). This post-translational modification determines the relative recruitment of either DNA repair or pro-apoptotic factors to the tail of serine phosphorylated histone H2AX (γ-H2AX) and allows it to function as an active determinant of repair/survival versus apoptotic responses to DNA damage, revealing an additional phosphorylation-dependent mechanism that modulates survival/apoptotic decisions during mammalian organogenesis.

Suggested Citation

  • Peter J. Cook & Bong Gun Ju & Francesca Telese & Xiangting Wang & Christopher K. Glass & Michael G. Rosenfeld, 2009. "Tyrosine dephosphorylation of H2AX modulates apoptosis and survival decisions," Nature, Nature, vol. 458(7238), pages 591-596, April.
    • Handle: RePEc:nat:nature:v:458:y:2009:i:7238:d:10.1038_nature07849
    DOI: 10.1038/nature07849
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    Cited by:

    1. Surbhi Chouhan & Dhivya Sridaran & Cody Weimholt & Jingqin Luo & Tiandao Li & Myles C. Hodgson & Luana N. Santos & Samantha Sommer & Bin Fang & John M. Koomen & Markus Seeliger & Cheng-Kui Qu & Armell, 2024. "SHP2 as a primordial epigenetic enzyme expunges histone H3 pTyr-54 to amend androgen receptor homeostasis," Nature Communications, Nature, vol. 15(1), pages 1-19, December.
    2. Jessica L. Kelliher & Melissa L. Folkerts & Kaiyuan V. Shen & Wan Song & Kyle Tengler & Clara M. Stiefel & Seong-Ok Lee & Eloise Dray & Weixing Zhao & Brian Koss & Nicholas R. Pannunzio & Justin W. Le, 2024. "Evolved histone tail regulates 53BP1 recruitment at damaged chromatin," Nature Communications, Nature, vol. 15(1), pages 1-14, December.

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