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Bax monomers form dimer units in the membrane that further self-assemble into multiple oligomeric species

MPG-Autoren
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Spatz,  Joachim P.
Cellular Biophysics, Max Planck Institute for Medical Research, Max Planck Society;
Biophysical Chemistry, Institute of Physical Chemistry, University of Heidelberg, 69120 Heidelberg, Germany;

Externe Ressourcen

http://www.nature.com/articles/ncomms9042.pdf
(beliebiger Volltext)

https://dx.doi.org/10.1038/ncomms9042
(beliebiger Volltext)

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Zitation

Subburaj, Y. D., Cosentino, K., Axmann, M., Pedruezza-Villalmanzo, E., Hermann, E., Bleicken, S., et al. (2015). Bax monomers form dimer units in the membrane that further self-assemble into multiple oligomeric species. Nature Communications, 6: 8042, pp. 1-11. doi:10.1038/ncomms9042.


Zitierlink: https://hdl.handle.net/11858/00-001M-0000-0028-8E60-8
Zusammenfassung
Bax is a key regulator of apoptosis that mediates the release of cytochrome c to the cytosol via oligomerization in the outer mitochondrial membrane before pore formation. However, the molecular mechanism of Bax assembly and regulation by other Bcl-2 members remains obscure. Here, by analysing the stoichiometry of Bax oligomers at the single-molecule level, we find that Bax binds to the membrane in a monomeric state and then self-assembles in <1 min. Strikingly, active Bax does not exist in a unique oligomeric state, but as several different species based on dimer units. Moreover, we show that cBid activates Bax without affecting its assembly, while Bcl-xL induces the dissociation of Bax oligomers. On the basis of our experimental data and theoretical modelling, we propose a new mechanism for the molecular pathway of Bax assembly to form the apoptotic pore.