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

Yamunadevi Subburaj, Katia Cosentino, Markus Axmann, Esteban Pedrueza-Villalmanzo, Eduard Hermann, Stephanie Bleicken, Joachim Spatz and Ana J. García-Sáez ()
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Yamunadevi Subburaj: Membrane Biophysics, Max Planck Institute for Intelligent Systems
Katia Cosentino: Membrane Biophysics, Max Planck Institute for Intelligent Systems
Markus Axmann: New Materials and Biosystems, Max Planck Institute for Intelligent Systems
Esteban Pedrueza-Villalmanzo: Membrane Biophysics, Max Planck Institute for Intelligent Systems
Eduard Hermann: Membrane Biophysics, Max Planck Institute for Intelligent Systems
Stephanie Bleicken: Membrane Biophysics, Max Planck Institute for Intelligent Systems
Joachim Spatz: New Materials and Biosystems, Max Planck Institute for Intelligent Systems
Ana J. García-Sáez: Membrane Biophysics, Max Planck Institute for Intelligent Systems

Nature Communications, 2015, vol. 6, issue 1, 1-11

Abstract: Abstract 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

Date: 2015
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DOI: 10.1038/ncomms9042

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