Sphingomyelin is much more effective than saturated phosphatidylcholine in excluding unsaturated phosphatidylcholine from domains formed with cholesterol

Duyl, Bianca Y. van; Ganchev, Dragomir N.; Chupin, Vladimir; Kruijff, Ben de; Killian, J. Antoinette

doi:10.1016/s0014-5793(03)00678-1

Cited by 93 publications

(69 citation statements)

References 34 publications

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“…phatidylcholine and sphingomyelin molecules, suggesting that these microdomains are enriched in sphingomyelin and likely exist in a liquid-ordered phase. These results were in good agreement with previous AFM reports on the spontaneous formation and thickness of cholesterol-and/or sphingomyelinrich lipid microdomains in supported lipid bilayers (49,50,53). The lipid microdomains were heterogeneous in size, ranging from ϳ50 to 500 nm in diameter, a size distribution that probably reflects lateral mobility and merger of smaller microdomains during the transition from liposomes to a supported bilayer (50).…”

Section: P14-induced Membrane Fusion Is Sensitive To Donorsupporting

confidence: 92%

The p14 Fusion-associated Small Transmembrane (FAST) Protein Effects Membrane Fusion from a Subset of Membrane Microdomains

Corcoran¹,

Salsman²,

Antueno³

et al. 2006

J. Biol. Chem.

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The reovirus fusion-associated small transmembrane (FAST) proteins are a unique family of viral membrane fusion proteins. These nonstructural viral proteins induce efficient cell-cell rather than virus-cell membrane fusion. We analyzed the lipid environment in which the reptilian reovirus p14 FAST protein resides to determine the influence of the cell membrane on the fusion activity of the FAST proteins. Topographical mapping of the surface of fusogenic p14-containing liposomes by atomic force microscopy under aqueous conditions revealed that p14 resides almost exclusively in thickened membrane microdomains. In transfected cells, p14 was found in both Lubrol WXand Triton X-100-resistant membrane complexes. Cholesterol depletion of donor cell membranes led to preferential disruption of p14 association with Lubrol WX (but not Triton X-100)-resistant membranes and decreased cell-cell fusion activity, both of which were reversed upon subsequent cholesterol repletion. Furthermore, co-patching analysis by fluorescence microscopy indicated that p14 did not co-localize with classical lipidanchored raft markers. These data suggest that the p14 FAST protein associates with heterogeneous membrane microdomains, a distinct subset of which is defined by cholesterol-dependent Lubrol WX resistance and which may be more relevant to the membrane fusion process.Biological membrane fusion is dependent on protein catalysts to mediate the lipid rearrangements required for membrane merger (1, 2). The fusion-associated small transmembrane (FAST) proteins are one such family of membrane fusion catalysts (3). The FAST proteins are a unique group of small (95-140 amino acids) integral membrane proteins encoded by the fusogenic reoviruses, an unusual group of non-enveloped viruses that induce syncytium formation (3-6). Three distinct members of the FAST protein family have been described in recent years: the homologous p10 proteins of avian reovirus and Nelson Bay reovirus and the unrelated p14 and p15 proteins of reptilian reovirus and baboon reovirus, respectively (3-5). Unlike the well characterized fusion proteins of enveloped viruses (7), the FAST proteins are nonstructural viral proteins and are therefore not involved in viral entry into cells. Following their expression inside virus-infected or -transfected cells, the FAST proteins traffic through the endoplasmic reticulum-Golgi pathway to assume a bitopic N exoplasmic /C cytoplasmic topology in the plasma membrane, where they mediate fusion of virus-infected cells to neighboring uninfected cells (8 -10). Therefore, the FAST proteins function more as "cellular" rather than viral fusion proteins, mediating cell-cell rather than viruscell membrane fusion. Furthermore, a recent study using the purified p14 FAST protein of reptilian reovirus reconstituted into artificial lipid bilayers indicated that the FAST proteins are both necessary and sufficient to mediate membrane fusion (11).In addition to their unique role in the viral replication cycle, the FAST proteins are also structurally ...

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Section: P14-induced Membrane Fusion Is Sensitive To Donorsupporting

confidence: 92%

The p14 Fusion-associated Small Transmembrane (FAST) Protein Effects Membrane Fusion from a Subset of Membrane Microdomains

Corcoran¹,

Salsman²,

Antueno³

et al. 2006

J. Biol. Chem.

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“…The small nanoscale domains previously observed with AFM by us and others (van Duyl et al, 2003) are found only when strong interactions with the support surface restrict lateral lipid mobility. However, there is growing evidence that functional microdomains in biological cells do in fact have nanoscale dimensions (Jacobson et al, 2007).…”

Section: Domain Coarsening In Ternary Membranessupporting

confidence: 57%

“…It is known from studies of free-standing membranes (Giant Unilamellar Vesicles-GUVs) that the membrane domains are 5-20 mm in diameter and circular due to line tension acting at the domain interfaces (Bagatolli, 2006). On the other hand, many studies of supported ternary membrane reveal much smaller (100-1000 nm) domains with very irregular shapes (van Duyl et al, 2003). This suggests that the membrane support may have a critical influence on the observed domains shapes.…”

Section: Resultsmentioning

confidence: 99%

Ligand–receptor interactions and membrane structure investigated by AFM and time‐resolved fluorescence microscopy

Thormann¹,

Simonsen²,

Nielsen³

et al. 2007

J of Molecular Recognition

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The atomic force microscope (AFM) and the associated dynamic force spectroscopy technique have been exploited to quantitatively assess the interaction between proteins and their binding to specific ligands and membrane surfaces. In particular, we have studied the specific interaction between lung surfactant protein D and various carbohydrates. In addition, we have used scanning AFM and time-resolved fluorescence microscopy to image the lateral structure of different lipid bilayers and their morphological changes as a function of time. The various systems studied illustrate the potential of modern AFM techniques for application to biomedical research, specifically within immunology and liposome-based drug delivery.

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“…Moreover, glycerolipids of plant DIM contain more saturated fatty acyl chains (Fig. 3B), which would contribute to the rigidity of the liquid-ordered phase of lipid rafts (42).…”

Section: Figmentioning

confidence: 99%

Lipid Rafts in Higher Plant Cells

Mongrand

Morel

Laroche

et al. 2004

Journal of Biological Chemistry

423

119

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A large body of evidence from the past decade supports the existence of functional microdomains in membranes of animal and yeast cells, which play important roles in protein sorting, signal transduction, or infection by pathogens. They are based on the dynamic clustering of sphingolipids and cholesterol or ergosterol and are characterized by their insolubility, at low temperature, in nonionic detergents. Here we show that similar microdomains also exist in plant plasma membrane isolated from both tobacco leaves and BY2 cells. Tobacco lipid rafts were found to be greatly enriched in a sphingolipid, identified as glycosylceramide, as well as in a mixture of stigmasterol, sitosterol, 24-methylcholesterol, and cholesterol. Phospho-and glycoglycerolipids of the plasma membrane were largely excluded from lipid rafts. Membrane proteins were separated by oneand two-dimensional gel electrophoresis and identified by tandem mass spectrometry or use of specific antibody. The data clearly indicate that tobacco microdomains are able to recruit a specific set of the plasma membrane proteins and exclude others. We demonstrate the recruitment of the NADPH oxidase after elicitation by cryptogein and the presence of the small G protein NtRac5, a negative regulator of NADPH oxidase, in lipid rafts.A new aspect of the lipid bilayer organization has arisen from biophysical and biochemical studies performed with animal cells for several years. Indeed, lipids are not uniformly miscible, but lateral separation of specific lipid species leads to the formation of specialized phase domains also called "lipid rafts" (1). The main role in the process of domain organization is played by sterols and sphingolipids, these latter interacting together through weak interaction between aliphatic chains stabilized by the presence of saturated alkyl chains, voids between sphingolipids being filled by sterols (for a review, see Ref.2). The cholesterol-sphingolipid-enriched domain formation is also enhanced by the fact that sphingolipids have higher melting temperatures than phospholipids. Regions between rafts are occupied by phospholipids, with unsaturated fatty acids forming a liquid-crystalline phase, whereas lipid rafts that contain more saturated aliphatic chains form a liquidordered phase. In model and biological membranes, the formation of the liquid-ordered phase correlates with resistance to solubilization by nonionic detergent such as Triton X-100 at 4°C and buoyancy at specific density in a sucrose gradient (3). Thus, isolation of detergent-insoluble membranes (DIM) 1 or detergent-insoluble glycolipid-enriched membrane domains is one of the most widely used methods for studying lipid rafts.In animal cells, these membrane domains act, for example, as sorting devices for the accumulation of acylated, glycosylphosphatidylinositol-anchored, palmitoylated signaling molecules that selectively locate in these domains. Tyrosine kinases of the Src family protein, heterotrimeric and small G-proteins, as well as phosphoinositides have been proved to be...

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Sphingomyelin is much more effective than saturated phosphatidylcholine in excluding unsaturated phosphatidylcholine from domains formed with cholesterol

Cited by 93 publications

References 34 publications

The p14 Fusion-associated Small Transmembrane (FAST) Protein Effects Membrane Fusion from a Subset of Membrane Microdomains

The p14 Fusion-associated Small Transmembrane (FAST) Protein Effects Membrane Fusion from a Subset of Membrane Microdomains

Ligand–receptor interactions and membrane structure investigated by AFM and time‐resolved fluorescence microscopy

Lipid Rafts in Higher Plant Cells

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