Mitochondria do not contain lipid rafts, and lipid rafts do not contain mitochondrial proteins

Zheng, Yu Zi; Berg, Kyra B.; Foster, Leonard J.

doi:10.1194/jlr.m800658-jlr200

Cited by 68 publications

(68 citation statements)

References 53 publications

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“…Rather than immediately subfractionating the postnuclear supernatant, we decided to include another step to clear the cholesterol-rich plasma membrane. This step was also introduced to remove mitochondria, which often end up as contaminating membranes in lipid microdomain isolation experiments ( 16 ). We reasoned that subjecting the postnuclear supernatant to short, intermediate-speed centrifugation might be sufficient to substantially remove large and dense organelles from the postnuclear supernatants, while buoyant and smaller vesicles, such as endosomes, would be less affected.…”

Section: Equilibrium Density Centrifugation Results In Incomplete Orgmentioning

confidence: 99%

Detergent-free isolation and characterization of cholesterol-rich membrane domains from trans-Golgi network vesicles

Waugh

Chu

Clayton

et al. 2011

Journal of Lipid Research

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Section: Equilibrium Density Centrifugation Results In Incomplete Orgmentioning

confidence: 99%

Detergent-free isolation and characterization of cholesterol-rich membrane domains from trans-Golgi network vesicles

Waugh

Chu

Clayton

et al. 2011

Journal of Lipid Research

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“…However, the presence of mitochondrial lipid rafts is still a matter of debate and characterization of the caspase-8/BID complex and the role of caridolipin in its function requires further clarification. 35 In summation, this novel caspase-8/BID mitochondrial complex concentrates the enzyme (caspase-8) and its substrate (BID) on the organelle where it is needed (mitochondria), thus providing a means by which the low levels of proteolytically active caspase-8 produced during type II apoptosis are able to efficiently engage the mitochondrial pathway.…”

Section: Discussionmentioning

confidence: 99%

BID is cleaved by caspase-8 within a native complex on the mitochondrial membrane

et al. 2010

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Caspase-8 stably inserts into the mitochondrial outer membrane during extrinsic apoptosis. Inhibition of caspase-8 enrichment on the mitochondria impairs caspase-8 activation and prevents apoptosis. However, the function of active caspase-8 on the mitochondrial membrane remains unknown. In this study, we have identified a native complex containing caspase-8 and BID on the mitochondrial membrane, and showed that death receptor activation by Fas or tumor necrosis factor-related apoptosisinducing ligand (TRAIL) induced the cleavage of BID (tBID formation) within this complex. tBID then shifted to separate mitochondria-associated complexes that contained other BCL-2 family members, such as BAK and BCL-X L . We report that cells stabilize active caspase-8 on the mitochondria in order to specifically target mitochondria-associated BID, and that BID cleavage on the mitochondria is essential for caspase-8-induced cytochrome c release. Our findings indicate that during extrinsic apoptosis, caspase-8 can specifically target BID where it is mostly needed, on the surface of mitochondria.

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“…Moreover, a recent study did not provide any evidence for the existence of detergent-resistant lipid rafts in mitochondrial membranes (Zheng et al, 2009). It is therefore an attractive possibility that different SPFH proteins stabilize membrane domains that differ in their phospholipid compositions.…”

Section: A Model For Prohibitins As Protein and Lipid Scaffoldsmentioning

confidence: 94%

Prohibitins and the functional compartmentalization of mitochondrial membranes

Osman

Merkwirth

Langer

2009

Journal of Cell Science

276

253

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Prohibitins constitute an evolutionarily conserved and ubiquitously expressed family of membrane proteins that are essential for cell proliferation and development in higher eukaryotes. Roles for prohibitins in cell signaling at the plasma membrane and in transcriptional regulation in the nucleus have been proposed, but pleiotropic defects associated with the loss of prohibitin genes can be largely attributed to a dysfunction of mitochondria. Two closely related proteins, prohibitin-1 (PHB1) and prohibitin-2 (PHB2), form large, multimeric ring complexes in the inner membrane of mitochondria. The absence of prohibitins leads to an increased generation of reactive oxygen species, disorganized mitochondrial nucleoids, abnormal cristae morphology and an increased sensitivity towards stimuli-elicited apoptosis. It has been found that the processing of the dynamin-like GTPase OPA1, which regulates mitochondrial fusion and cristae morphogenesis, is a key process regulated by prohibitins. Furthermore, genetic analyses in yeast have revealed an intimate functional link between prohibitin complexes and the membrane phospholipids cardiolipin and phosphatidylethanolamine. In light of these findings, it is emerging that prohibitin complexes can function as protein and lipid scaffolds that ensure the integrity and functionality of the mitochondrial inner membrane.

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Mitochondria do not contain lipid rafts, and lipid rafts do not contain mitochondrial proteins

Cited by 68 publications

References 53 publications

Detergent-free isolation and characterization of cholesterol-rich membrane domains from trans-Golgi network vesicles

Detergent-free isolation and characterization of cholesterol-rich membrane domains from trans-Golgi network vesicles

BID is cleaved by caspase-8 within a native complex on the mitochondrial membrane

Prohibitins and the functional compartmentalization of mitochondrial membranes

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