APOOL is a cardiolipin-binding constituent of the Mitofilin/MINOS protein complex determining cristae morphology in mammalian mitochondria

Mitochondrial cristae morphology is highly variable and altered under numerous pathological conditions. The protein complexes involved are largely unknown or only insufficiently characterized. Using complexome profiling we identified apolipoprotein O (APOO) and apolipoprotein O-like protein (APOOL)...

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Published in:	PloS one 2013-05, Vol.8 (5), p.e63683-e63683
Main Authors:	Weber, Tobias A, Koob, Sebastian, Heide, Heinrich, Wittig, Ilka, Head, Brian, van der Bliek, Alexander, Brandt, Ulrich, Mittelbronn, Michel, Reichert, Andreas S
Format:	Article
Language:	eng
Subjects:	Animals Apolipoproteins Apolipoproteins - metabolism Apoptosis B cells Binding Bioenergetics Biology Biosynthesis Cardiolipin Cardiolipins - metabolism Cattle Cristae Down-Regulation Electron transport HeLa Cells Humans Life sciences Lipids Mammals Mammals - metabolism Membrane lipids Membrane proteins Membrane Proteins - metabolism Metabolism Mitochondria Mitochondria - metabolism Mitochondria - ultrastructure Mitochondria, Heart - metabolism Mitochondria, Heart - ultrastructure Mitochondrial Membranes - metabolism Mitochondrial Membranes - ultrastructure Mitochondrial Proteins - metabolism Morphology Multiprotein Complexes - metabolism Muscle Proteins - metabolism Oxygen Oxygen Consumption Phosphatidylglycerol Protein Binding Proteins
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Summary:	Mitochondrial cristae morphology is highly variable and altered under numerous pathological conditions. The protein complexes involved are largely unknown or only insufficiently characterized. Using complexome profiling we identified apolipoprotein O (APOO) and apolipoprotein O-like protein (APOOL) as putative components of the Mitofilin/MINOS protein complex which was recently implicated in determining cristae morphology. We show that APOOL is a mitochondrial membrane protein facing the intermembrane space. It specifically binds to cardiolipin in vitro but not to the precursor lipid phosphatidylglycerol. Overexpression of APOOL led to fragmentation of mitochondria, a reduced basal oxygen consumption rate, and altered cristae morphology. Downregulation of APOOL impaired mitochondrial respiration and caused major alterations in cristae morphology. We further show that APOOL physically interacts with several subunits of the MINOS complex, namely Mitofilin, MINOS1, and SAMM50. We conclude that APOOL is a cardiolipin-binding component of the Mitofilin/MINOS protein complex determining cristae morphology in mammalian mitochondria. Our findings further assign an intracellular role to a member of the apolipoprotein family in mammals.
ISSN:	1932-6203 1932-6203