p53 SUMOylation promotes its nuclear export by facilitating its release from the nuclear export receptor CRM1

@inproceedings{Santiago2013p53SP,
  title={p53 SUMOylation promotes its nuclear export by facilitating its release from the nuclear export receptor CRM1},
  author={A. P{\'e}rez Santiago and Dawei Li and Lisa Y. Zhao and Adam C Godsey and Daiqing Liao},
  booktitle={Molecular biology of the cell},
  year={2013}
}
Chromosomal region maintenance 1 (CRM1) mediates p53 nuclear export. Although p53 SUMOylation promotes its nuclear export, the underlying mechanism is unclear. Here we show that tethering of a small, ubiquitin-like modifier (SUMO) moiety to p53 markedly increases its cytoplasmic localization. SUMO attachment to p53 does not affect its oligomerization, suggesting that subunit dissociation required for exposing p53's nuclear export signal (NES) is unnecessary for p53 nuclear export. Surprisingly… CONTINUE READING

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CRM1-mediated nuclear export: to the pore and beyond.

Trends in cell biology • 2007
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Highly Influenced

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