Stomatin-like protein 2 binds cardiolipin and regulates mitochondrial biogenesis and function |
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Authors: | Christie Darah A Lemke Caitlin D Elias Isaac M Chau Luan A Kirchhof Mark G Li Bo Ball Eric H Dunn Stanley D Hatch Grant M Madrenas Joaquín |
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Affiliation: | The Centre for Human Immunology, Robarts Research Institute, Department of Microbiology and Immunology, and Department of Medicine, The University of Western Ontario, London, Ontario, Canada. |
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Abstract: | Stomatin-like protein 2 (SLP-2) is a widely expressed mitochondrial inner membrane protein of unknown function. Here we show that human SLP-2 interacts with prohibitin-1 and -2 and binds to the mitochondrial membrane phospholipid cardiolipin. Upregulation of SLP-2 expression increases cardiolipin content and the formation of metabolically active mitochondrial membranes and induces mitochondrial biogenesis. In human T lymphocytes, these events correlate with increased complex I and II activities, increased intracellular ATP stores, and increased resistance to apoptosis through the intrinsic pathway, ultimately enhancing cellular responses. We propose that the function of SLP-2 is to recruit prohibitins to cardiolipin to form cardiolipin-enriched microdomains in which electron transport complexes are optimally assembled. Likely through the prohibitin functional interactome, SLP-2 then regulates mitochondrial biogenesis and function. |
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