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

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.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-70E2-5 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-7BE7-9
Genre: Journal Article

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 Creators:
Große, L.1, Author              
Wurm, C. A.1, Author              
Brüser, C.2, Author              
Neumann, D.2, Author              
Jans, D. C.2, Author              
Jakobs, S.2, Author              
Affiliations:
1Department of NanoBiophotonics, MPI for Biophysical Chemistry, Max Planck Society, ou_578627              
2Research Group of Mitochondrial Structure and Dynamics, MPI for biophysical chemistry, Max Planck Society, ou_578566              

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Free keywords: Bcl-2; cell death; membrane curvature; MICOS; superresolution microscopy
 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.

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Language(s): eng - English
 Dates: 2016-01-182016-02-15
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.15252/embj.201592789
 Degree: -

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Title: EMBO Journal
Source Genre: Journal
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Pages: - Volume / Issue: 35 (4) Sequence Number: - Start / End Page: 402 - 413 Identifier: -