BH3‐in‐groove dimerization initiates and helix 9 dimerization expands Bax pore assembly in membranes
Open accessAbstract
Pro-apoptotic Bax induces mitochondrial outer membrane permeabilization (MOMP) by forming oligomers through a largely undefined process. Using site-specific disulfide crosslinking, compartment-specific chemical labeling, and mutational analysis, we found that activated integral membrane Bax proteins form a BH3-in-groove dimer interface on the MOM surface similar to that observed in crystals. However, after the α5 helix was released into the MOM, the remaining interface with α2, α3, and α4 helices was rearranged. Another dimer interface was formed inside the MOM by two intersected or parallel α9 helices. Combinations of these interfaces generated oligomers in the MOM. Oligomerization was initiated by BH3-in-groove dimerization, without which neither the other dimerizations nor MOMP occurred. In contrast, α9 dimerization occurred downstream and was required for release of large but not small proteins from mitochondria. Moreover, the release of large proteins was facilitated by α9 insertion into the MOM and localization to the pore rim. Therefore, the BH3-in-groove dimerization on the MOM nucleates the assembly of an oligomeric Bax pore that is enlarged by α9 dimerization at the rim.
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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 [80]
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- Authors
- Zhang, Z., Subramaniam, S., Kale, J., Liao, C., Huang, B., Brahmbhatt, H., Condon, S. G., Lapolla, S. M., Hays, F. A., Ding, J., He, F., Zhang, X. C., Li, J., Senes, A., Andrews, D. W., & Lin, J.
- Affiliations
- University of Oklahoma Health Sciences Center (US)
- University of Wisconsin–Madison (US)
- University of Toronto (CA)
- University of Vermont (US)
- Chinese Academy of Sciences (CN)
- OU Health Stephenson Cancer Center (US)
- Corresponding author
- Lin, Jialing
- ORCID
- Venue
- The EMBO Journal
- Published
- 2015-12-23
- Volume
- 35
- Issue
- 2
- Pages
- 208-236
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC4718459
- OpenAlex
- W2219794611
- Cited by
- 93
- References
- 65
- Citations by year
- 2026: 2 · 2025: 7 · 2024: 3 · 2023: 6 · 2022: 9 · 2021: 13 · 2020: 8 · 2019: 9 · 2018: 10 · 2017: 18 · 2016: 8
- FWCI
- 5.21
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The EMBO Journal (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- NIH (R01GM062964, R01GM099752, P20GM104934, P20GM103639)
- OCAST (HR10‐121)
- NSF (CHE‐1415910, ACI‐1053575)
- NLM (5T15LM007359)
- CIHR (FRN12517)
- 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, mitochondrial outer membrane permeabilization, Bax oligomerization, mitochondrial outer membrane, apoptosis, disulfide cross-linking, protein-protein interaction
- MeSH terms
- Animals, Cell Line, Protein Binding, Apoptosis, Dimerization, Immunoprecipitation, bcl-2 Homologous Antagonist-Killer Protein, bcl-2-Associated X Protein, Mitochondrial Membranes
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