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

• DOI: 10.1091/mbc.e11-09-0774
• Publication Date: 2011-11-24T05:55:38Z
• Authors: Alwaleed K. Alkhaja; Daniel C. Jans; Miroslav Nikolov; Milena Vukotic; Oleksandr Lytovch...; Fabian Ludewig; Wolfgang Schliebs; Dietmar Riedel; Henning Urlaub; Stefan Jakobs; Markus Deckers
• Keywords: 0301 basic medicine; Saccharomyces cerevisiae Proteins; Molecular Sequence Data; Membrane Proteins; Muscle Proteins; Articles; Saccharomyces cerevisiae; Mitochondria; Mitochondrial Proteins; Proton-Translocating ATPases; 03 medical and health sciences; HEK293 Cells; Mitochondrial Membranes; Humans; Amino Acid Sequence

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.