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Mol Biol Cell. 2012 Jan;23(2):247-57. doi: 10.1091/mbc.E11-09-0774. Epub 2011 Nov 23.

MINOS1 is a conserved component of mitofilin complexes and required for mitochondrial function and cristae organization.

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  • 1Department of Biochemistry II, University of Göttingen Medical School, D-37073 Göttingen, Germany.

Abstract

The inner membrane of mitochondria is especially protein rich and displays a unique morphology characterized by large invaginations, the mitochondrial cristae, and the inner boundary membrane, which is in proximity to the outer membrane. Mitochondrial inner membrane proteins appear to be not evenly distributed in the inner membrane, but instead organize into functionally distinct subcompartments. It is unknown how the organization of the inner membrane is achieved. We identified MINOS1/MIO10 (C1orf151/YCL057C-A), a conserved mitochondrial inner membrane protein. mio10-mutant yeast cells are affected in growth on nonfermentable carbon sources and exhibit altered mitochondrial morphology. At the ultrastructural level, mutant mitochondria display loss of inner membrane organization. Proteomic analyses reveal MINOS1/Mio10 as a novel constituent of Mitofilin/Fcj1 complexes in human and yeast mitochondria. Thus our analyses reveal new insight into the composition of the mitochondrial inner membrane organizing machinery.

PMID:
22114354
[PubMed - indexed for MEDLINE]
PMCID:
PMC3258170
Free PMC Article

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