ArticleBiophysical journal2014
The proapoptotic protein tBid forms both superficially bound and membrane-inserted oligomers.
Article in Biophysical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers, 1 of them a synthesis that pooled it.
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Who cites it
15 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Calpain Inhibitors as Potential Therapeutic Modulators in Neurodegenerative Diseases.Neurochemical research · 2022Pooled it
- The minimal membrane requirements for BAX-induced pore opening upon exposure to oxidative stress.Biophysical journal · 2024Article
- The C-terminal sequences of Bcl-2 family proteins mediate interactions that regulate cell death.The Biochemical journal · 2024Review
- Canonical and Noncanonical Functions of the BH3 Domain Protein Bid in Apoptosis, Oncogenesis, Cancer Therapeutics, and Aging.Cancers · 2024Review
- 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
- Direct Measurement of the Affinity between tBid and Bax in a Mitochondria-Like Membrane.International journal of molecular sciences · 2021Article
- Stepwise activation of the pro-apoptotic protein Bid at mitochondrial membranes.Cell death and differentiation · 2021Article
- Accessing local structural disruption of Bid protein during thermal denaturation by absorption-mode ESR spectroscopy.RSC advances · 2018Article
- Humanin decreases mitochondrial membrane permeability by inhibiting the membrane association and oligomerization of Bax and Bid proteins.Acta pharmacologica Sinica · 2018Article
- Mitochondrial outer membrane permeabilization: a focus on the role of mitochondrial membrane structural organization.Biophysical reviews · 2017Review
- Quantitative interactome of a membrane Bcl-2 network identifies a hierarchy of complexes for apoptosis regulation.Nature communications · 2017Article
- Bcl-2 proteins bid and bax form a network to permeabilize the mitochondria at the onset of apoptosis.Cell death & disease · 2016Article
- Article
- Effect of Cholesterol on the Structure of a Five-Component Mitochondria-Like Phospholipid Membrane.Membranes · 2015Article
- In situ quantification of protein binding to the plasma membrane.Biophysical journal · 2015Article
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Authors and funding
10 authors.
Funding
Abstract
Bid is a proapopotic activator protein of the Bcl-2 family that plays a pivotal role in controlling mitochondrial outer membrane permeabilization during apoptosis. Here, we characterized the interaction of fluorescently labeled truncated Bid (tBid) with a mitochondria-like supported lipid bilayer at the single-molecule level. The proteins observed at the membrane exhibited a very wide range of mobility. Confocal images of the membrane displayed both diffraction-limited Gaussian spots and horizontal streaks, corresponding to immobile and mobile tBid species, respectively. We observed 1), fast-diffusing proteins corresponding to a loosely, probably electrostatically bound state; 2), slowly diffusing proteins, likely corresponding to a superficially inserted state; and 3), fully immobilized proteins, suggesting a fully inserted state. The stoichiometry of these proteins was determined by normalizing their fluorescence intensity by the brightness of a tBid monomer, measured separately using fluorescence fluctuation techniques. Strikingly, the immobile species were found to be mainly tetramers and higher, whereas the mobile species had on average a significantly lower stoichiometry. Taken together, these results show that as soluble Bid progresses toward a membrane-inserted state, it undergoes an oligomerization process similar to that observed for Bax.
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