Bax monomers form dimer units in the membrane that further self-assemble into multiple oligomeric species
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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.
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Activated BAX and BAK form homodimers (also heterodimers in specific settings), resulting in the release of BH3-only proteins and further dimer-by-dimer oligomerization.
“The current view is that activated BAX and BAK form homodimers (also heterodimers in specific settings), resulting in the release of BH3-only proteins and further dimer-by-dimer oligomerization [76–83].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [79]
Most pro-survival BCL2 family members inhibit BAX and BAK by preventing their oligomerization and pore-forming activity either directly, upon physical sequestration at the OMM, or indirectly, following the sequestration of BH3-only activators.
“Thus, most pro-survival BCL2 family members inhibit BAX and BAK by preventing their oligomerization and pore-forming activity either directly, upon physical sequestration at the OMM, or indirectly, following the sequestration of BH3-only activators [29, 64, 79, 110].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [79]
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References 59 · Cited by 181
Research works printed but not linked: 1
- Loman, A., Mu ¨ller, C. B., Koberling, F., Richtering, W. & Enderlein, J. in 14th International Workshop on Single Molecule Spectroscopy and Ultrasensitive Analysis in Life Sciences (Berlin, 2008).
- Authors
- Subburaj, Y., Cosentino, K., Axmann, M., Pedrueza-Villalmanzo, E., Hermann, E., Bleicken, S., Spatz, J., & García-Sáez, A. J.
- Affiliations
- Max Planck Institute for Intelligent Systems (DE)
- Venue
- Nature Communications
- Published
- 2015-08-14
- Volume
- 6
- Issue
- 1
- Pages
- 8042-8042
- ISSN
- 2041-1723 (ISSN-L)
- PMC
- PMC4557355
- OpenAlex
- W1915252789
- Cited by
- 181
- References
- 59
- Citations by year
- 2026: 8 · 2025: 12 · 2024: 15 · 2023: 15 · 2022: 17 · 2021: 18 · 2020: 13 · 2019: 12 · 2018: 18 · 2017: 28 · 2016: 19 · 2015: 5
- FWCI
- 10.13
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Nature Communications (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- IRIS UNIMORE (University of Modena and Reggio Emilia) (submittedVersion, cc-by)
- RePEc: Research Papers in Economics (submittedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion)
- Funders
- Deutsche Forschungsgemeinschaft (FOR‐2036, 309966, DFG FOR 2036, ZUK63)
- Austrian Science Fund (J 3086, FOR-2036)
- Max-Planck-Gesellschaft
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Keywords
- Bax, Bax oligomerization, cytochrome c release, mitochondrial outer membrane, Bcl-2 family proteins, Bcl-xL, single-molecule analysis, apoptosis
- MeSH terms
- Lipid Bilayers, Microscopy, Protein Binding, Spectrometry, Fluorescence, bcl-2-Associated X Protein
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