期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 114, 期 2, 页码 310-315出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1612322114
关键词
apoptosis; Bcl-2; mitochondria; oligomerization; transmembrane
资金
- Spanish Ministry of Economy and Competitiveness [BFU2016-79487, SAF2014-52614-R, BEFPI/2013/A/046]
- Generalitat Valenciana Grant [PROMETEOII/2014/061]
- Emmy Noether program
- Heisenberg program
- German Research Council (Deutsche Forschungsgemeinschaft) [Sonderforschungsbereich 746]
- Centre for Biological Signalling Studies (BIOSS) - Excellence Initiative of the German Federal and State Governments [EXC-294]
- Generalitat Valenciana [BEFPI/2013/A/046, ACIF/2016/019]
The Bcl-2 (B-cell lymphoma 2) protein Bax (Bcl-2 associated X, apoptosis regulator) can commit cells to apoptosis via outer mitochondrial membrane permeabilization. Bax activity is controlled in healthy cells by prosurvival Bcl-2 proteins. C-terminal Bax transmembrane domain interactions were implicated recently in Bax pore formation. Here, we show that the isolated transmembrane domains of Bax, Bcl-xL (B-cell lymphoma-extra large), and Bcl-2 can mediate interactions between Bax and prosurvival proteins inside the membrane in the absence of apoptotic stimuli. Bcl-2 protein transmembrane domains specifically homooligomerize and heterooligomerize in bacterial and mitochondrial membranes. Their interactions participate in the regulation of Bcl-2 proteins, thus modulating apoptotic activity. Our results suggest that interactions between the transmembrane domains of Bax and antiapoptotic Bcl-2 proteins represent a previously unappreciated level of apoptosis regulation.
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