ArticleGenes & development2007
A three-helix homo-oligomerization domain containing BH3 and BH1 is responsible for the apoptotic activity of Bax.
Article in Genes & development, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 82 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
82 citing papers in PubMed, 125 citations in OpenAlex.
- A gated hydrophobic funnel within BAX binds bioactive lipids to potentiate pro-apoptotic function.Nature communications · 2026Article
- Activator of apoptosis harakiri (HRK) localisation at mitochondria alters mitochondrial morphology independently of other BCL-2 proteins.The FEBS journal · 2026Article
- The C-terminal sequences of Bcl-2 family proteins mediate interactions that regulate cell death.The Biochemical journal · 2024Review
- A BAK subdomain that binds mitochondrial lipids selectively and releases cytochrome C.Cell death and differentiation · 2023Article
- The Bak core dimer focuses triacylglycerides in the membrane.Biophysical journal · 2022Article
- BH3-mimetics: recent developments in cancer therapy.Journal of experimental & clinical cancer research : CR · 2021Review
- Dynamic reconfiguration of pro-apoptotic BAK on membranes.The EMBO journal · 2021Article
- The conformational stability of pro-apoptotic BAX is dictated by discrete residues of the protein core.Nature communications · 2021Article
- Transient Unfolding and Long-Range Interactions in Viral BCL2 M11 Enable Binding to the BECN1 BH3 Domain.Biomolecules · 2020Article
- The third model of Bax/Bak activation: a Bcl-2 family feud finally resolved?F1000Research · 2020Review
- BH3-only proteins target BCL-xL/MCL-1, not BAX/BAK, to initiate apoptosis.Cell research · 2019Article
- Fundamental Mechanisms of Regulated Cell Death and Implications for Heart Disease.Physiological reviews · 2019Review
- Synthesis of Chalcone Derivatives: Inducing Apoptosis of HepG2 CellsFrontiers in pharmacology · 2019Article
- Up-regulation of hexokinase II contributes to rituximab-chemotherapy resistance and is a clinically relevant target for therapeutic development.Oncotarget · 2018Article
- The BCL-2 arbiters of apoptosis and their growing role as cancer targets.Cell death and differentiation · 2018Review
- Subcellular Localization and Dynamics of the Bcl-2 Family of Proteins.Frontiers in cell and developmental biology · 2018Review
- Virus Infection and Death Receptor-Mediated Apoptosis.Viruses · 2017Review
- The functional domains for Bax∆2 aggregate-mediated caspase 8-dependent cell death.Experimental cell research · 2017Article
- A novel chalcone derivative S17 induces apoptosis through ROS dependent DR5 up-regulation in gastric cancer cells.Scientific reports · 2017Article
- Release of Cytochrome C from Bax Pores at the Mitochondrial Membrane.Scientific reports · 2017Article
22 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Homo-oligomerization of Bax (or Bak) has been hypothesized to be responsible for cell death through the mitochondria-dependent apoptosis pathway. However, partly due to a lack of structural information on the Bax homo-oligomerization and apoptosis inducing domain(s), this hypothesis has remained difficult to test. In this study, we identified a three-helix unit, comprised of the BH3 (helix 2) and BH1 domains (helix 4 and helix 5), as the homo-oligomerization domain of Bax. When targeted to mitochondria, this minimum oligomerization unit induced apoptosis in Bax(-/-)Bak(-/-) mouse embryonic fibroblasts (DKO). Strikingly, the central helix of Bax (helix 5), when replacing the corresponding helix (helix 5) of Bcl-xL, an anti-apoptotic Bcl-2 family protein structurally homologous to Bax, converted Bcl-xL into a Bax-like molecule capable of forming oligomers and causing apoptosis in the DKO cells. Finally, a series of systematic mutagenesis analyses revealed that homo-oligomerization is both necessary and sufficient for the apoptotic activity of Bax. These results suggest that active Bax causes mitochondrial damage through homo-oligomers of a three-helix functional unit.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.