Specific requirements of nonbilayer phospholipids in mitochondrial respiratory chain function and formation

Mitochondrial membrane phospholipid composition affects mitochondrial function by influencing the assembly of the mitochondrial respiratory chain (MRC) complexes into supercomplexes. For example, the loss of cardiolipin (CL), a signature non-bilayer-forming phospholipid of mitochondria, results in d...

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Bibliographic Details
Published in:Molecular biology of the cell 2016-07, Vol.27 (14), p.2161-2171
Main Authors: Baker, Charli D, Basu Ball, Writoban, Pryce, Erin N, Gohil, Vishal M
Format: Article
Language:English
Subjects:
Cardiolipins - metabolism
Electron Transport - physiology
Endoplasmic Reticulum - metabolism
Mitochondria - metabolism
Mitochondrial Membranes - metabolism
Phosphatidylcholines - metabolism
Phosphatidylethanolamines - metabolism
Phospholipids - metabolism
Saccharomyces cerevisiae - metabolism
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Summary:Mitochondrial membrane phospholipid composition affects mitochondrial function by influencing the assembly of the mitochondrial respiratory chain (MRC) complexes into supercomplexes. For example, the loss of cardiolipin (CL), a signature non-bilayer-forming phospholipid of mitochondria, results in disruption of MRC supercomplexes. However, the functions of the most abundant mitochondrial phospholipids, bilayer-forming phosphatidylcholine (PC) and non-bilayer-forming phosphatidylethanolamine (PE), are not clearly defined. Using yeast mutants of PE and PC biosynthetic pathways, we show a specific requirement for mitochondrial PE in MRC complex III and IV activities but not for their formation, whereas loss of PC does not affect MRC function or formation. Unlike CL, mitochondrial PE or PC is not required for MRC supercomplex formation, emphasizing the specific requirement of CL in supercomplex assembly. Of interest, PE biosynthesized in the endoplasmic reticulum (ER) can functionally substitute for the lack of mitochondrial PE biosynthesis, suggesting the existence of PE transport pathway from ER to mitochondria. To understand the mechanism of PE transport, we disrupted ER-mitochondrial contact sites formed by the ERMES complex and found that, although not essential for PE transport, ERMES facilitates the efficient rescue of mitochondrial PE deficiency. Our work highlights specific roles of non-bilayer-forming phospholipids in MRC function and formation.
ISSN:1059-1524
1939-4586
DOI:10.1091/mbc.e15-12-0865