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Biochim Biophys Acta. 2009 Oct;1788(10):2084-91. doi: 10.1016/j.bbamem.2009.04.003. Epub 2009 Apr 14.

Cardiolipin membrane domains in prokaryotes and eukaryotes.

Author information

1
Department of Biochemistry and Molecular Biology, University of Texas Medical School, Houston, TX 77030, USA. Eugenia.Mileykovskaya@uth.tmc.edu

Abstract

Cardiolipin (CL) plays a key role in dynamic organization of bacterial and mitochondrial membranes. CL forms membrane domains in bacterial cells, and these domains appear to participate in binding and functional regulation of multi-protein complexes involved in diverse cellular functions including cell division, energy metabolism, and membrane transport. Visualization of CL domains in bacterial cells by the fluorescent dye 10-N-nonyl acridine orange is critically reviewed. Possible mechanisms proposed for CL dynamic localization in bacterial cells are discussed. In the mitochondrial membrane CL is involved in organization of multi-subunit oxidative phosphorylation complexes and in their association into higher order supercomplexes. Evidence suggesting a possible role for CL in concert with ATP synthase oligomers in establishing mitochondrial cristae morphology is presented. Hypotheses on CL-dependent dynamic re-organization of the respiratory chain in response to changes in metabolic states and CL dynamic re-localization in mitochondria during the apoptotic response are briefly addressed.

PMID:
19371718
PMCID:
PMC2757463
DOI:
10.1016/j.bbamem.2009.04.003
[Indexed for MEDLINE]
Free PMC Article

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