Caspase-dependent deubiquitination of monoubiquitinated nucleosomal histone H2A induced by diverse apoptogenic stimuli

@article{Mimnaugh2001CaspasedependentDO,
  title={Caspase-dependent deubiquitination of monoubiquitinated nucleosomal histone H2A induced by diverse apoptogenic stimuli},
  author={Edward G. Mimnaugh and Ganesh L Kayastha and Nicola McGovern and S-G Hwang and Monica G Marcu and Jane B. Trepel and S Cai and Vincent T. Marchesi and Leonard M. Neckers},
  journal={Cell Death and Differentiation},
  year={2001},
  volume={8},
  pages={1182-1196}
}
Enzymatic deubiquitination of mono-ubiquitinated nucleosomal histone H2A (uH2A) and H2B (uH2B) is closely associated with mitotic chromatin condensation, although the function of this histone modification in cell division remains ambiguous. Here we show that rapid and extensive deubiquitination of nucleosomal uH2A occurs in Jurkat cells undergoing apoptosis initiated by anti-Fas activating antibody, staurosporine, etoposide, doxorubicin and the proteasome inhibitor, N-acetyl-leucyl-leucyl… CONTINUE READING