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  Mic10 Oligomerization Pinches off Mitochondrial Cristae

Milenkovic, D., & Larsson, N. (2015). Mic10 Oligomerization Pinches off Mitochondrial Cristae. Cell Metab, 21(5), 660-1. doi:10.1016/j.cmet.2015.04.020.

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Item Permalink: https://hdl.handle.net/21.11116/0000-000B-7AE2-D Version Permalink: https://hdl.handle.net/21.11116/0000-000B-7AE3-C
Genre: Journal Article

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https://www.ncbi.nlm.nih.gov/pubmed/25955201 (Any fulltext)
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 Creators:
Milenkovic, D.1, Author           
Larsson, N.G.1, Author           
Affiliations:
1Department Larsson - Mitochondrial Biology, Max Planck Institute for Biology of Ageing, Max Planck Society, ou_1942286              

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Free keywords: Membrane Proteins/*metabolism Mitochondria/*metabolism/*ultrastructure Mitochondrial Membranes/*metabolism Mitochondrial Proteins/*metabolism Saccharomyces cerevisiae/*cytology/*metabolism Saccharomyces cerevisiae Proteins/*metabolism
 Abstract: The mitochondrial contact site and cristae organizing system (MICOS) complex is essential for normal mitochondria biogenesis and morphology. In this issue, Bohnert et al. (2015) and Barbot et al. (2015) demonstrate that a MICOS core subunit, Mic10, is crucial for mitochondrial cristae formation by forming oligomers at the cristae junctions.

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 Dates: 2015-05-052015-05-09
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: Other: 25955201
DOI: 10.1016/j.cmet.2015.04.020
ISSN: 1550-4131
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Title: Cell Metab
  Alternative Title : Cell metabolism
Source Genre: Journal
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Pages: - Volume / Issue: 21 (5) Sequence Number: - Start / End Page: 660 - 1 Identifier: -