Bax monomers form dimer units in the membrane that further self-assemble into multiple oligomeric species

Bax is a key regulator of apoptosis that mediates the release of cytochrome c to the cytosol via oligomerization in the outer mitochondrial membrane before pore formation. However, the molecular mechanism of Bax assembly and regulation by other Bcl-2 members remains obscure. Here, by analysing the s...

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Bibliographic Details
Published in:Nature communications 2015-08, Vol.6 (1), p.8042-8042, Article 8042
Main Authors: Subburaj, Yamunadevi, Cosentino, Katia, Axmann, Markus, Pedrueza-Villalmanzo, Esteban, Hermann, Eduard, Bleicken, Stephanie, Spatz, Joachim, García-Sáez, Ana J.
Format: Article
Language:English
Subjects:
631/57/2271
631/57/2272
631/80/82/23
631/80/86
bcl-2-Associated X Protein - chemistry
bcl-2-Associated X Protein - metabolism
Humanities and Social Sciences
Lipid Bilayers
Microscopy - methods
multidisciplinary
Protein Binding
Science
Science (multidisciplinary)
Spectrometry, Fluorescence - methods
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Summary:Bax is a key regulator of apoptosis that mediates the release of cytochrome c to the cytosol via oligomerization in the outer mitochondrial membrane before pore formation. However, the molecular mechanism of Bax assembly and regulation by other Bcl-2 members remains obscure. Here, by analysing the stoichiometry of Bax oligomers at the single-molecule level, we find that Bax binds to the membrane in a monomeric state and then self-assembles in
ISSN:2041-1723
2041-1723
DOI:10.1038/ncomms9042