ArticleThe Journal of biological chemistry2010
Bax forms an oligomer via separate, yet interdependent, surfaces.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 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
49 citing papers in PubMed, 77 citations in OpenAlex.
- Mammalian innate antiviral defenses: beyond interferon.Journal of virology · 2025Review
- Profiling protein-protein interactions to predict the efficacy of B-cell-lymphoma-2-homology-3 mimetics for acute myeloid leukaemia.Nature biomedical engineering · 2024Article
- Study of the Bcl-2 Interactome by BiFC Reveals Differences in the Activation Mechanism of Bax and Bak.Cells · 2023Article
- Structure-destabilizing mutations unleash an intrinsic perforation activity of antiapoptotic Bcl-2 in the mitochondrial membrane enabling apoptotic cell death.Mitochondrial communications · 2023Article
- Dynamic reconfiguration of pro-apoptotic BAK on membranes.The EMBO journal · 2021Article
- Intrinsically Connected: Therapeutically Targeting the Cathepsin Proteases and the Bcl-2 Family of Protein Substrates as Co-regulators of Apoptosis.International journal of molecular sciences · 2021Review
- Cysteine-based crosslinking approach for characterization of oligomeric pore-forming proteins in the mitochondrial membranes.Methods in enzymology · 2021Article
- Pore formation in regulated cell death.The EMBO journal · 2020Review
- Lipids glue BAK dimers together.Nature structural & molecular biology · 2020Article
- BAX, BAK, and BOK: A Coming of Age for the BCL-2 Family Effector Proteins.Cold Spring Harbor perspectives in biology · 2020Review
- The carboxyl-terminal sequence of bim enables bax activation and killing of unprimed cells.eLife · 2020Article
- Parkin inhibits BAK and BAX apoptotic function by distinct mechanisms during mitophagy.The EMBO journal · 2019Article
- Photocrosslinking Approach to Investigate Protein Interactions in the BCL-2 Family.Methods in molecular biology (Clifton, N.J.) · 2019Article
- Topology of active, membrane-embedded Bax in the context of a toroidal pore.Cell death and differentiation · 2018Article
- The functional domains for Bax∆2 aggregate-mediated caspase 8-dependent cell death.Experimental cell research · 2017Article
- Pore formation by dimeric Bak and Bax: an unusual pore?Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017Review
- BAK α6 permits activation by BH3-only proteins and homooligomerization via the canonical hydrophobic groove.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- A Small-Molecule Inhibitor of Bax and Bak Oligomerization Prevents Genotoxic Cell Death and Promotes Neuroprotection.Cell chemical biology · 2017Article
- Article
- Bax transmembrane domain interacts with prosurvival Bcl-2 proteins in biological membranes.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
Corrections and comments
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Authors and funding
13 authors at 4 institutions in 2 countries.
Funding
Abstract
Interactions of Bcl-2 family proteins regulate permeability of the mitochondrial outer membrane and apoptosis. In particular, Bax forms an oligomer that permeabilizes the membrane. To map the interface of the Bax oligomer we used Triton X-100 as a membrane surrogate and performed site-specific photocross-linking. Bax-specific adducts were formed through photo-reactive probes at multiple sites that can be grouped into two surfaces. The first surface overlaps with the BH1-3 groove formed by Bcl-2 Homology motif 1, 2, and 3; the second surface is a rear pocket located on the opposite side of the protein from the BH1-3 groove. Further cross-linking experiments using Bax BH3 peptides and mutants demonstrated that the two surfaces interact with their counterparts in neighboring proteins to form two separated interfaces and that interaction at the BH1-3 groove primes the rear pocket for further interaction. Therefore, Bax oligomerization proceeds through a series of interactions that occur at separate, yet allosterically, coupled interfaces.
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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.