MST1 promotes apoptosis through phosphorylation of histone H2AX.

  title={MST1 promotes apoptosis through phosphorylation of histone H2AX.},
  author={Wei-hong Wen and Feng Zhu and Jishuai Zhang and Y. W. Keum and Tatyana A. Zykova and Ke Yao and C. Ray Peng and Duo Zheng and Yong-Yeon Cho and Wei-ya Ma and Ann M. Bode and Ziming Dong},
  journal={The Journal of biological chemistry},
  volume={285 50},
MST1 (mammalian STE20-like kinase 1) is a serine/threonine kinase that is cleaved and activated by caspases during apoptosis. Overexpression of MST1 induces apoptotic morphological changes such as chromatin condensation, but the mechanism is not clear. Here we show that MST1 induces apoptotic chromatin condensation through its phosphorylation of histone H2AX at Ser-139. During etoposide-induced apoptosis in Jurkat cells, the cleavage of MST1 directly corresponded with strong H2AX… CONTINUE READING
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