Biochemistry Publications
Document Type
Article
Publication Date
9-1-2011
Journal
Molecular and cellular biology
Volume
31
Issue
18
First Page
3845
Last Page
3856
URL with Digital Object Identifier
http://dx.doi.org/10.1128/MCB.05393-11
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.
Notes
http://dx.doi.org/10.1128/MCB.05393-11