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Beclin 1 cleavage by caspase-3 inactivates autophagy and promotes apoptosis

Open access
Zhu, Yushan, Zhao, Lixia, Liu, Lei, Gao, Ping, Tian, Weili, Wang, Xiaohui, Jin, Haijing, Xu, Haidong, Chen, Quan·2010·Protein & Cell

Abstract

Autophagy and apoptosis are both highly regulated biological processes that play essential roles in tissue homeostasis, development and diseases. Autophagy is also described as a mechanism of death pathways, however, the precise mechanism of how autophagy links to cell death remains to be fully understood. Beclin 1 is a dual regulator for both autophagy and apoptosis. In this study we found that Beclin 1 was a substrate of caspase-3 with two cleavage sites at positions 124 and 149, respectively. Furthermore, the autophagosome formation occurred, followed by the appearance of morphological hallmarks of apoptosis after staurosporine treatment. The cleavage products of Beclin 1 reduced autophagy and promoted apoptosis in HeLa cells and the cells in which Beclin 1 was stably knocked down by specific shRNA. In addition, the cleavage of Beclin 1 resulted in abrogating the interaction between Bcl-2 with Beclin 1, which could be blocked by z-VAD-fmk. Thus, our results suggest that the cleavage of Beclin 1 by caspase-3 may contribute to inactivate autophagy leading towards augmented apoptosis.

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Metadata

Authors
Zhu, Y., Zhao, L., Liu, L., Gao, P., Tian, W., Wang, X., Jin, H., Xu, H., & Chen, Q.
Venue
Protein & Cell
Published
2010-05
Volume
1
Issue
5
Pages
468-477
ISSN
  • 1674-800X (ISSN-L)
  • 1674-8018
OpenAlex
W1983467638
Cited by
254
References
4
FWCI
7.13
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: Beclin 1 cleavage by caspase-3 inactivates autophagy and promotes apoptosis. https://app.cochat.ai/papers/10.1007/s13238-010-0048-4
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Zhu, Y., Zhao, L., Liu, L., Gao, P., Tian, W., Wang, X., Jin, H., Xu, H., & Chen, Q. (2010). Beclin 1 cleavage by caspase-3 inactivates autophagy and promotes apoptosis. Protein & Cell. https://doi.org/10.1007/s13238-010-0048-4

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