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  Mic10 oligomerizes to bend mitochondrial inner membranes at cristae junctions.

Barbot, M., Jans, D. C., Schulz, C., Denkert, N., Kroppen, B., Hoppert, M., et al. (2015). Mic10 oligomerizes to bend mitochondrial inner membranes at cristae junctions. Cell Metabolism, 21(5), 756-763. doi:10.1016/j.cmet.2015.04.006.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-12A6-3 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-51AC-C
Genre: Journal Article

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 Creators:
Barbot, M., Author
Jans, D. C.1, Author              
Schulz, C., Author
Denkert, N., Author
Kroppen, B., Author
Hoppert, M., Author
Jakobs, S.1, Author              
Meinecke, M., Author
Affiliations:
1Research Group of Mitochondrial Structure and Dynamics, MPI for biophysical chemistry, Max Planck Society, ou_578566              

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 Abstract: The mitochondrial inner membrane is highly folded and displays a complex molecular architecture. Cristae junctions are highly curved tubular openings that separate cristae membrane invaginations from the surrounding boundary membrane. Despite their central role in many vital cellular processes like apoptosis, the details of cristae junction formation remain elusive. Here we identify Mic10, a core subunit of the recently discovered MICOS complex, as an inner mitochondrial membrane protein with the ability to change membrane morphology in vitro and in vivo. We show that Mic10 spans the inner membrane in a hairpin topology and that its ability to sculpt membranes depends on oligomerization through a glycine-rich motif. Oligomerization mutants fail to induce curvature in model membranes, and when expressed in yeast, mitochondria display an altered inner membrane architecture characterized by drastically decreased numbers of cristae junctions. Thus, we demonstrate that membrane sculpting by Mic10 is essential for cristae junction formation.

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Language(s): eng - English
 Dates: 2015-05-05
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1016/j.cmet.2015.04.006
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Title: Cell Metabolism
Source Genre: Journal
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Pages: - Volume / Issue: 21 (5) Sequence Number: - Start / End Page: 756 - 763 Identifier: -