Stomatin-like protein 2 binds cardiolipin and regulates mitochondrial biogenesis and function.
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Christie DA, Lemke CD, Elias IM, Chau LA, Kirchhof MG, Li B, Ball EH, Dunn SD, Hatch GM, Madrenas J
Stomatin-like protein 2 binds cardiolipin and regulates mitochondrial biogenesis and function.
Mol Cell Biol. 2011 Sep;31(18):3845-56. doi: 10.1128/MCB.05393-11. Epub 2011 Jul 11.
- PubMed ID
- 21746876 [ View in PubMed]
- 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.