Abstract
As a critical apoptosis executioner, caspase-3 becomes activated and then enters into the nucleus to exert its function. However, the molecular mechanism of this nuclear entry of active caspase-3 is still unknown. In this study, we revealed that caspase-3 harbors a crm-1-independent nuclear export signal (NES) in its small subunit. Using reverse-caspase-3 as the study model, we found that the function of the NES in caspase-3 was not disturbed by the conformational changes during induced caspase-3 activation. Mutations disrupting the cleavage activity or p3-recognition site resulted in a defect in the nuclear entry of active caspase-3. We provide evidence that the p3-mediated specific cleavage activity of active caspase-3 abrogated the function of the NES. In conclusion, our results demonstrate that during caspase-3 activation, NES is constitutively present. p3-mediated specific cleavage activity abrogates the NES function in caspase-3, thus facilitating the nuclear entry of active caspase-3.
Original language | English (US) |
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Pages (from-to) | 211-222 |
Number of pages | 12 |
Journal | Cell Research |
Volume | 20 |
Issue number | 2 |
DOIs | |
State | Published - Feb 2010 |
Keywords
- Apoptosis
- Caspase-3
- Nuclear entry
- Nuclear export signal
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology