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Nuclear entry of active caspase-3 is facilitated by its p3-recognition-based specific cleavage activity
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Nuclear entry of active caspase-3 is facilitated by its p3-recognition-based specific cleavage activity
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Journal Article
Nuclear entry of active caspase-3 is facilitated by its p3-recognition-based specific cleavage activity
2010
Overview
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 easpase-3 harbors a crm-l-independent nuclear export signal （NES） in its small subunit. Using reversecaspase-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.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ Active Transport, Cell Nucleus - physiology
/ Biomedical and Life Sciences
/ caspase
/ CRM
/ Enzyme Activation - genetics
/ Humans
/ Mutation
/ Nuclear Export Signals - genetics
/ Nuclear Export Signals - physiology
/ Protein Processing, Post-Translational - physiology
/ Protein Subunits - chemistry
/ Protein Subunits - metabolism
/ Receptors, Cytoplasmic and Nuclear - metabolism
/ 分子机制
/ 切割活性
/ 断裂活动
/ 活性构象
/ 细胞凋亡
