Structure-destabilizing mutations unleash an intrinsic perforation activity of antiapoptotic Bcl-2 in the mitochondrial membrane enabling apoptotic cell death

Structure-destabilizing mutations unleash an intrinsic perforation activity of antiapoptotic Bcl-2 in the mitochondrial membrane enabling apoptotic cell death

Bcl-2 and Bax share a similar structural fold in solution, yet function oppositely in the mitochondrial outer membrane (MOM) during apoptosis. The proapoptotic Bax forms pores in the MOM to trigger cell death, whereas Bcl-2 inhibits the Bax pore formation to prevent cell death. Intriguingly both pro...

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Bibliographic Details
Main Authors: Ping Gao, Zhi Zhang, Rui Wang, Li Huang, Hao Wu, Zhenzhen Qiao, Xiaohui Wang, Haijing Jin, Jun Peng, Lei Liu, Quan Chen, Jialing Lin
Format: Article
Language:English
Published: KeAi Communications Co., Ltd. 2023-01-01
Series:Mitochondrial Communications
Subjects:
Bcl-2 protein pore
Mitochondrial membrane
Cytochrome c release
Apoptosis
Online Access:http://www.sciencedirect.com/science/article/pii/S2590279223000044
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