Dephosphorylation and caspase processing generate distinct nuclear pools of histone deacetylase 4.

@article{Paroni2007DephosphorylationAC,
  title={Dephosphorylation and caspase processing generate distinct nuclear pools of histone deacetylase 4.},
  author={Gabriela Paroni and Alessandra Fontanini and Nadia Cernotta and Carmela Foti and M. V. N. V. Prasad Gupta and X M Yang and Dario Fasino and Claudio Brancolini},
  journal={Molecular and cellular biology},
  year={2007},
  volume={27 19},
  pages={6718-32}
}
From the nucleus, histone deacetylase 4 (HDAC4) regulates a variety of cellular processes, including growth, differentiation, and survival, by orchestrating transcriptional changes. Extracellular signals control its repressive influence mostly through regulating its nuclear-cytoplasmic shuttling. In particular, specific posttranslational modifications such as phosphorylation and caspase-mediated proteolytic processing operate on HDAC4 to promote its nuclear accumulation or export. To understand… CONTINUE READING
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