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Journal Article

Bax assembles into large ring-like structures remodeling the mitochondrial outer membrane in apoptosis.

MPS-Authors
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Große,  L.
Department of NanoBiophotonics, MPI for Biophysical Chemistry, Max Planck Society;

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Wurm,  C. A.
Department of NanoBiophotonics, MPI for Biophysical Chemistry, Max Planck Society;

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Brüser,  C.
Research Group of Mitochondrial Structure and Dynamics, MPI for biophysical chemistry, Max Planck Society;

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Neumann,  D.
Research Group of Mitochondrial Structure and Dynamics, MPI for biophysical chemistry, Max Planck Society;

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Jans,  D. C.
Research Group of Mitochondrial Structure and Dynamics, MPI for biophysical chemistry, Max Planck Society;

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Jakobs,  S.
Research Group of Mitochondrial Structure and Dynamics, MPI for biophysical chemistry, Max Planck Society;

Fulltext (public)

2246280.pdf
(Publisher version), 4MB

2246280_Suppl_7.zip
(Publisher version), 134KB

Supplementary Material (public)

2246280_Suppl_1.pdf
(Supplementary material), 642KB

2246280_Suppl_2.pdf
(Supplementary material), 232KB

2246280_Suppl_3.zip
(Supplementary material), 255MB

2246280_Suppl_4.zip
(Supplementary material), 123KB

2246280_Suppl_5.zip
(Supplementary material), 5MB

2246280_Suppl_6.zip
(Supplementary material), 146MB

Citation

Große, L., Wurm, C. A., Brüser, C., Neumann, D., Jans, D. C., & Jakobs, S. (2016). Bax assembles into large ring-like structures remodeling the mitochondrial outer membrane in apoptosis. EMBO Journal, 35(4), 402-413. doi:10.15252/embj.201592789.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0029-70E2-5
Abstract
The Bcl-2 family proteins Bax and Bak are essential for the execution of many apoptotic programs. During apoptosis, Bax translocates to the mitochondria and mediates the permeabilization of the outer membrane, thereby facilitating the release of pro-apoptotic proteins. Yet the mechanistic details of the Baxinduced membrane permeabilization have so far remained elusive. Here, we demonstrate that activated Bax molecules, besides forming large and compact clusters, also assemble, potentially with other proteins including Bak, into ring-like structures in the mitochondrial outer membrane. STED nanoscopy indicates that the area enclosed by a Bax ring is devoid of mitochondrial outer membrane proteins such as Tom20, Tom22, and Sam50. This strongly supports the view that the Bax rings surround an opening required for mitochondrial outer membrane permeabilization (MOMP). Even though these Bax assemblies may be necessary for MOMP, we demonstrate that at least in Drp1 knockdown cells, these assemblies are not sufficient for full cytochrome c release. Together, our super-resolution data provide direct evidence in support of large Bax-delineated pores in the mitochondrial outer membrane as being crucial for Bax-mediated MOMP in cells.