Quantitative interactome of a membrane Bcl-2 network identifies a hierarchy of complexes for apoptosis regulation
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The Bcl-2 proteins form a complex interaction network that controls mitochondrial permeabilization and apoptosis. The relative importance of different Bcl-2 complexes and their spatio-temporal regulation is debated. Using fluorescence cross-correlation spectroscopy to quantify the interactions within a minimal Bcl-2 network, comprised by cBid, Bax, and Bcl-xL, we show that membrane insertion drastically alters the pattern of Bcl-2 complexes, and that the C-terminal helix of Bcl-xL determines its binding preferences. At physiological temperature, Bax can spontaneously activate in a self-amplifying process. Strikingly, Bax also recruits Bcl-xL to membranes, which is sufficient to retrotranslocate Bax back into solution to secure membrane integrity. Our study disentangles the hierarchy of Bcl-2 complex formation in relation to their environment: Bcl-xL association with cBid occurs in solution and in membranes, where the complex is stabilized, whereas Bcl-xL binding to Bax occurs only in membranes and with lower affinity than to cBid, leading instead to Bax retrotranslocation.
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In physiological conditions, some anti-apoptotic BCL2 proteins, such as BCL-XL, exert a protective role by promoting the retrotranslocation of BAX and (to a lesser degree) BAK from the mitochondria to the cytoplasm, thus limiting their mitochondrial pool.
“Of note, in physiological conditions, some anti-apoptotic BCL2 proteins, such as BCL-XL, exert a protective role by promoting the retrotranslocation of BAX and (to a lesser degree) BAK from the mitochondria to the cytoplasm, thus limiting their mitochondrial pool [48, 55, 111].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [111]
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- Authors
- Bleicken, S., Hantusch, A., Das, K. K., Frickey, T., & Garcia-Saez, A. J.
- Affiliations
- German Cancer Research Center (DE)
- University of Konstanz (DE)
- University of Tübingen (DE)
- Venue
- Nature Communications
- Published
- 2017-07-13
- Volume
- 8
- Issue
- 1
- Pages
- 73-73
- ISSN
- 2041-1723 (ISSN-L)
- PMC
- PMC5509671
- OpenAlex
- W2727592297
- Cited by
- 70
- References
- 75
- Citations by year
- 2026: 5 · 2025: 7 · 2024: 6 · 2023: 11 · 2022: 2 · 2021: 11 · 2020: 11 · 2019: 5 · 2018: 9 · 2017: 3
- FWCI
- 3.13
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Nature Communications (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, other-oa)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- KOPS (University of Konstanz) (submittedVersion, cc-by)
- Funders
- Deutsches Krebsforschungszentrum
- Deutsche Forschungsgemeinschaft (309966, EXC 1069)
- Bundesministerium für Bildung und Forschung (0312040, EXC 1069)
- Max-Planck-Gesellschaft (EXC 1069)
- 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
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Keywords
- Bcl-2 family proteins, apoptosis regulation, mitochondrial membrane permeabilization, Bax, Bcl-xL, membrane insertion, protein-protein interaction, fluorescence cross-correlation spectroscopy
- MeSH terms
- Animals, Cell Membrane, Humans, Models, Chemical, Protein Binding, Apoptosis, bcl-2-Associated X Protein, Mice, Unilamellar Liposomes
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