Please use this identifier to cite or link to this item: http://hdl.handle.net/10397/20940
Title: Nuclear entry of active caspase-3 is facilitated by its p3-recognition-based specific cleavage activity
Authors: Luo, M
Lu, Z
Sun, H
Yuan, K
Zhang, Q
Meng, S
Wang, F
Guo, H
Ju, X
Liu, Y
Ye, T 
Lu, Z
Zhai, Z
Keywords: Apoptosis
Caspase-3
Nuclear entry
Nuclear export signal
Issue Date: 2010
Publisher: Inst Biochemistry & Cell Biology
Source: Cell research, 2010, v. 20, no. 2, p. 211-222 How to cite?
Journal: Cell Research 
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.
URI: http://hdl.handle.net/10397/20940
DOI: 10.1038/cr.2010.9
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