ArticleScientific reports2016
Assembly of Bak homodimers into higher order homooligomers in the mitochondrial apoptotic pore.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- The BCL-2 protein family: from discovery to drug development.Cell death and differentiation · 2025Review
- Mechanisms of BCL-2 family proteins in mitochondrial apoptosis.Nature reviews. Molecular cell biology · 2023Review
- Apoptotic mitochondrial poration by a growing list of pore-forming BCL-2 family proteins.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023Article
- Protein-protein and protein-lipid interactions of pore-forming BCL-2 family proteins in apoptosis initiation.Biochemical Society transactions · 2022Review
- Structural basis of BAK activation in mitochondrial apoptosis initiation.Nature communications · 2022Article
- High-resolution analysis of the conformational transition of pro-apoptotic Bak at the lipid membrane.The EMBO journal · 2021Article
- NF-κB activity during pancreas development regulates adult β-cell mass by modulating neonatal β-cell proliferation and apoptosis.Cell death discovery · 2021Article
- Pore formation in regulated cell death.The EMBO journal · 2020Review
- BAK core dimers bind lipids and can be bridged by them.Nature structural & molecular biology · 2020Article
- On the Stability and Degradation Pathways of Venetoclax under Stress Conditions.Pharmaceutics · 2020Article
- Robust autoactivation for apoptosis by BAK but not BAX highlights BAK as an important therapeutic target.Cell death & disease · 2020Article
- BAX, BAK, and BOK: A Coming of Age for the BCL-2 Family Effector Proteins.Cold Spring Harbor perspectives in biology · 2020Review
- Overcoming Resistance to Therapies Targeting the MAPK Pathway in BRAF-Mutated Tumours.Journal of oncology · 2020Review
- A new perspective on membrane-embedded Bax oligomers using DEER and bioresistant orthogonal spin labels.Scientific reports · 2019Article
- Topology of active, membrane-embedded Bax in the context of a toroidal pore.Cell death and differentiation · 2018Article
- Contribution of BH3-domain and Transmembrane-domain to the Activity and Interaction of the Pore-forming Bcl-2 Proteins Bok, Bak, and Bax.Scientific reports · 2018Article
- BH3-Dependent and Independent Activation of BAX and BAK in Mitochondrial Apoptosis.Current opinion in physiology · 2018Article
- BCL-2 family proteins: changing partners in the dance towards death.Cell death and differentiation · 2018Review
- Membrane insertion of the BAX core, but not latch domain, drives apoptotic pore formation.Scientific reports · 2017Article
- Pore formation by dimeric Bak and Bax: an unusual pore?Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017Review
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Authors and funding
9 authors.
Funding
Abstract
In mitochondrial apoptosis, Bak is activated by death signals to form pores of unknown structure on the mitochondrial outer membrane via homooligomerization. Cytochrome c and other apoptotic factors are released from the intermembrane space through these pores, initiating downstream apoptosis events. Using chemical crosslinking and double electron electron resonance (DEER)-derived distance measurements between specific structural elements in Bak, here we clarify how the Bak pore is assembled. We propose that previously described BH3-in-groove homodimers (BGH) are juxtaposed via the 'α3/α5' interface, in which the C-termini of helices α3 and α5 are in close proximity between two neighboring Bak homodimers. This interface is observed concomitantly with the well-known 'α6:α6' interface. We also mapped the contacts between Bak homodimers and the lipid bilayer based on EPR spectroscopy topology studies. Our results suggest a model for the lipidic Bak pore, whereby the mitochondrial targeting C-terminal helix does not change topology to accommodate the lining of the pore lumen by BGH.
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