Author
Listed:
- Yamunadevi Subburaj
(Membrane Biophysics, Max Planck Institute for Intelligent Systems)
- Katia Cosentino
(Membrane Biophysics, Max Planck Institute for Intelligent Systems
Membrane Biophysics, Interfaculty Institute of Biochemistry, University of Tuebingen)
- Markus Axmann
(New Materials and Biosystems, Max Planck Institute for Intelligent Systems
Present address: Institute for Applied Physics—Biophysics, Vienna University of Technology, Getreidemarkt 9, A-1060 Wien, Austria)
- Esteban Pedrueza-Villalmanzo
(Membrane Biophysics, Max Planck Institute for Intelligent Systems
Membrane Biophysics, Interfaculty Institute of Biochemistry, University of Tuebingen)
- Eduard Hermann
(Membrane Biophysics, Max Planck Institute for Intelligent Systems
Membrane Biophysics, Interfaculty Institute of Biochemistry, University of Tuebingen)
- Stephanie Bleicken
(Membrane Biophysics, Max Planck Institute for Intelligent Systems
Membrane Biophysics, Interfaculty Institute of Biochemistry, University of Tuebingen)
- Joachim Spatz
(New Materials and Biosystems, Max Planck Institute for Intelligent Systems)
- Ana J. García-Sáez
(Membrane Biophysics, Max Planck Institute for Intelligent Systems
Membrane Biophysics, Interfaculty Institute of Biochemistry, University of Tuebingen)
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
Suggested Citation
Yamunadevi Subburaj & Katia Cosentino & Markus Axmann & Esteban Pedrueza-Villalmanzo & Eduard Hermann & Stephanie Bleicken & Joachim Spatz & Ana J. García-Sáez, 2015.
"Bax monomers form dimer units in the membrane that further self-assemble into multiple oligomeric species,"
Nature Communications, Nature, vol. 6(1), pages 1-11, November.
Handle:
RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms9042
DOI: 10.1038/ncomms9042
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