The first alpha helix of Bax plays a necessary role in its ligand-induced activation by the BH3-only proteins Bid and PUMA.
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Summary
A specific interaction between Bax Halpha1 and their BH3 domains allows Bid and PUMA to function as "death agonists" of Bax, whereas Bad recruits Bax activity through a distinct pathway.
- Type
- article
- Published
- 2004-12-03
- Cited by
- 278
- References
- 25
- Access
- Open access
- OpenAlex
- https://openalex.org/W1965071591
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:27712582
Keywords
Puma, Biology, Helix (gastropod), Ligand (biochemistry), Cell biology
References
- Structure of Bax: coregulation of dimer formation and intracellular localization.
- Apoptotic pathways: paper wraps stone blunts scissors.
- tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome c.
- Cleavage of Bax to p18 Bax accelerates stress-induced apoptosis, and a cathepsin-like protease may rapidly degrade p18 Bax.
- Minimal BH3 Peptides Promote Cell Death by Antagonizing Anti-apoptotic Proteins*
- Distinct BH3 domains either sensitize or activate mitochondrial apoptosis, serving as prototype cancer therapeutics.
- Keeping killers on a tight leash: transcriptional and post-translational control of the pro-apoptotic activity of BH3-only proteins
- tBID Homooligomerizes in the Mitochondrial Membrane to Induce Apoptosis*
- Proapoptotic BAX and BAK: A Requisite Gateway to Mitochondrial Dysfunction and Death
- The Bcl-2 protein family: sensors and checkpoints for life-or-death decisions.
- No PUMA, no death: implications for p53-dependent apoptosis.
- Bax-induced cytochrome c release from mitochondria depends on alpha-helices-5 and -6.
- Involvement of the N‐terminus of Bax in its intracellular localization and function
- Bid, Bax, and lipids cooperate to form supramolecular openings in the outer mitochondrial membrane.
- The p18 Truncated Form of Bax Behaves Like a Bcl-2 Homology Domain 3-only Protein*
- Bid-induced Conformational Change of Bax Is Responsible for Mitochondrial Cytochrome c Release during Apoptosis
- The Bcl-2 protein family.
- The N-terminal End of Bax Contains a Mitochondrial-targeting Signal*
- Bid induces cytochrome c-impermeable Bax channels in liposomes.
- BID: a novel BH3 domain-only death agonist.
Cited by
- Role of Bcl-2 Family Members in Anoxia Induced Cell Death
- BH3‐only proteins: The death‐puppeteer's wires
- NEW INSIGHTS INTO THE REGULATION OF MITOCHONDRIAL OUTER MEMBRANE PERMEABILIZATION DURING APOPTOSIS
- Platinum resistant cancer cells conserve sensitivity to BH3 domains and obatoclax induced mitochondrial apoptosis
- Implication de l'extrémité C-terminale de Bax dans son homo-oligomérisation au cours de l'apoptose
- Yeast as a model system for the study of Bax regulation by protein kinase C isoforms
- Functional Role of Glycogen synthase Kinase-3β on Glucocorticoid-mediated signaling
- Approche combinée expérimentale et mathématique pour la personnalisation sur base moléculaire des thérapies anticancéreuses standards et chronomodulées. (A combined experimental and mathematical approach for molecular-based personalization of chronomodulated and standard anticancer therapies)
- Regulation of BAX/BAK-Dependent Cell Death Program
- Determining the role of endothelial progenitor cells in post-natal neovascularization
- The mitochondrial pathways of apoptosis.
- Regulation of programmed cell death by the p53 pathway.
- Targeting survival pathways in lymphoma.
- A C-terminus Mitochondrial-localization Region and BH3 Domain of Puma are Required for Apoptotic Function
- Mécanismes moléculaires de l'acquisition d'une sensibilité à l'apoptose induite par l'ABT-737 et d'une résistance à l'anoïkis de cellules coliques métastatiques
- GALIG : UN NOUVEAU GÈNE HUMAIN INDUCTEUR DE LA MORT CELLULAIRE
- Mise en évidence d'un marqueur de bon pronostic dans le glioblastome multiforme, l'enzyme mPGES-1 : identification de son produit PGE2 comme un nouvel activateur direct de la protéine pro-apoptotique Bax
- Régulation de l’apoptose dépendante de p53 par le FGF1 intracellulaire : caractérisation des mécanismes d’action
- FCS Analysis of Pore Formation by the Human Protein Bax in Lipid Membranes
- Flexibility and specificity of the interaction of MCL-1 with BIM BH3
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