Spontaneous lipid transfer between organized lipid assemblies

Brown, Rhoderick E.

doi:10.1016/0304-4157(92)90007-w

Cited by 93 publications

(74 citation statements)

References 151 publications

(270 reference statements)

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“…Upon increasing the concentration of acceptor membrane, no increase in the transfer rate of MG12AO was observed. This invariance of transfer rate to acceptor is a hallmark of an aqueous diffusion transfer mechanism for hydrophobic compounds (49,50). We also found that increasing the NaCl concentration of the buffer reduced the rate of MG12AO transfer from LFABP logarithmically, suggesting that the solvation properties of the surrounding aqueous phase regulate the movement of MG from LFABP to membranes.…”

Section: Discussionmentioning

confidence: 61%

Liver Fatty Acid-binding Protein Binds Monoacylglycerol in Vitro and in Mouse Liver Cytosol

Lagakos

Guan

et al. 2013

Journal of Biological Chemistry

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Section: Discussionmentioning

confidence: 61%

Liver Fatty Acid-binding Protein Binds Monoacylglycerol in Vitro and in Mouse Liver Cytosol

Lagakos

Guan

et al. 2013

Journal of Biological Chemistry

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“…Schuck et al (Schuck et al, 2003) show that DRM isolation using the non-ionic detergent Triton X-100 results in the isolation of the least number of proteins in the insoluble fractions compared with other detergents tested. Therefore, we based our criteria for DRM-resident proteins on this stringent method: insolubility in Triton X-100 at 4°C and buoyancy in sucrose gradients (Brown, 1992;Schuck et al, 2003). Western blotting of equal proportions (by volume) of low-density, insoluble and soluble fractions using 10E6 revealed that erlin-1 was highly enriched in the DRMs of both the U937 and 3T3-erlin-1 cell lines (Fig.…”

Section: Resultsmentioning

confidence: 99%

Erlin-1 and erlin-2 are novel members of the prohibitin family of proteins that define lipid-raft-like domains of the ER

Browman

Resek

Zajchowski

et al. 2006

Journal of Cell Science

198

204

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Our laboratory was interested in characterizing the molecular composition of non-caveolar lipid rafts. Thus, we generated monoclonal antibodies to lipid raft proteins of human myelomonocytic cells. Two of these proteins, KE04p and C8orf2, were found to be highly enriched in the detergent-insoluble, buoyant fraction of sucrose gradients in a cholesterol-dependent manner. They contain an evolutionarily conserved domain placing them in the prohibitin family of proteins. In contrast to other family members, these two proteins localized to the ER. Furthermore, the extreme N-termini of KE04p and C8orf2 were found to be sufficient for heterologous targeting of GFP to the ER in the absence of classical ER retrieval motifs. We also demonstrate that all prohibitin family members rely on sequences in their extreme N-termini for their distinctive subcellular distributions including the mitochondria, plasma membrane and Golgi vesicles. Owing to their subcellular localization and their presence in lipid rafts, we have named KE04p and C8orf2, ER lipid raft protein (erlin)-1 and erlin-2, respectively. Interestingly, the ER contains relatively low levels of cholesterol and sphingolipids compared with other organelles. Thus, our data support the existence of lipid-raft-like domains within the membranes of the ER.

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“…Indeed, evidence has been presented that GlcCer (and not SM) still reached the plasma membrane when vesicular tra¤c was inhibited by brefeldin A [255]. Because the spontaneous exchange of GlcCer, SM, and other glycosphingolipids through the water phase is very slow (half-time of days [292]), transfer would be expected to occur at sites of close membrane contact [293] or it should be stimulated by the presence of glycosphingolipid transfer proteins. Such a protein has been isolated from cytosol [294,295], and its cDNA has been cloned [296].…”

Section: Monomeric Exchangementioning

confidence: 99%

Sphingolipid transport in eukaryotic cells

Meer

Holthuis

2000

Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biolog

152

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Sphingolipids constitute a sizeable fraction of the membrane lipids in all eukaryotes and are indispensable for eukaryotic life. First of all, the involvement of sphingolipids in organizing the lateral domain structure of membranes appears essential for processes like protein sorting and membrane signaling. In addition, recognition events between complex glycosphingolipids and glycoproteins are thought to be required for tissue differentiation in higher eukaryotes and for other specific cell interactions. Finally, upon certain stimuli like stress or receptor activation, sphingolipids give rise to a variety of second messengers with effects on cellular homeostasis. All sphingolipid actions are governed by their local concentration. The intricate control of their intracellular topology by the proteins responsible for their synthesis, hydrolysis and intracellular transport is the topic of this review. ß

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Spontaneous lipid transfer between organized lipid assemblies

Cited by 93 publications

References 151 publications

Liver Fatty Acid-binding Protein Binds Monoacylglycerol in Vitro and in Mouse Liver Cytosol

Liver Fatty Acid-binding Protein Binds Monoacylglycerol in Vitro and in Mouse Liver Cytosol

Erlin-1 and erlin-2 are novel members of the prohibitin family of proteins that define lipid-raft-like domains of the ER

Sphingolipid transport in eukaryotic cells

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