Cardiolipin membrane domains in prokaryotes and eukaryotes.
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.
Department of Biochemistry and Molecular Biology, University of Texas Medical School, Houston, TX 77030, USA. Eugenia.Mileykovskaya@uth.tmc.edu
Eugenia
E
Mileykovskaya
William
W
Dowhan
D000818:Animals; D002308:Cardiolipins / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism*; D005057:Eukaryotic Cells / Q000378:metabolism*; D006801:Humans; D011387:Prokaryotic Cells / Q000378:metabolism*
D002308:Cardiolipins