Looking at lipid rafts?

Jacobson, Kenneth A.; Dietrich, Christian

doi:10.1016/s0962-8924(98)01495-0

Cited by 395 publications

(292 citation statements)

References 32 publications

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“…It has been suggested that lipid rafts may be disrupted by antibody binding (Anderson, 1998;Jacobson and Dietrich, 1999;Kurzchalia and Parton, 1999). However, most data indicate that antibody binding and cross-linking do not disrupt (our unpublished results) (Mayor and Maxfield, 1995;Kenworthy and Edidin, 1998) and indeed may stabilize (Harder et al, 1998) the association of proteins with lipid rafts.…”

Section: Discussionmentioning

confidence: 65%

“…Cross-linking or other perturbations aggregate the complexes and stabilize them. Variations of these models have been described previously (Harder and Simons, 1997;Simons and Ikonen, 1997;Brown and London, 1998;Jacobson and Dietrich, 1999). See the text for details of how FRET microscopy measurements can discriminate between these models.…”

Section: Plasma Membrane Distribution Of Lipid Raft Markers Detected mentioning

confidence: 99%

“…The relationship between membrane extracts and the in vivo composition and structure of lipid rafts is uncertain and controversial (Kurzchalia et al, 1995;Edidin, 1997;Harder and Simons, 1997;Simons and Ikonen, 1997;Weimbs et al, 1997;Brown and London, 1998;Hooper, 1998;Jacobson and Dietrich, 1999). One might expect that lipid rafts would concentrate molecules such as GPI-anchored proteins, effectively clustering them.…”

Section: Introductionmentioning

confidence: 99%

“…In other cases clusters of GPI-anchored proteins or other lipid raft components are only apparent when they have been crosslinked with secondary antibodies (Howell et al 1987;Rothberg et al, 1990;Fra et al, 1994;Mayor et al, 1994;Parton et al, 1994;Fujimoto, 1996;Harder et al, 1998). This suggests that in vivo, lipid rafts may be small or dynamic structures that are aggregated and stabilized by detergent extraction or by antibody-induced cross-linking (Edidin, 1997;Harder and Simons, 1997;Simons and Ikonen, 1997;Weimbs et al, 1997;Brown and London, 1998;Jacobson and Dietrich, 1999).…”

Section: Introductionmentioning

confidence: 99%

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High-Resolution FRET Microscopy of Cholera Toxin B-Subunit and GPI-anchored Proteins in Cell Plasma Membranes

Kenworthy

Petranova

Edidin

2000

MBoC

406

311

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“Lipid rafts” enriched in glycosphingolipids (GSL), GPI-anchored proteins, and cholesterol have been proposed as functional microdomains in cell membranes. However, evidence supporting their existence has been indirect and controversial. In the past year, two studies used fluorescence resonance energy transfer (FRET) microscopy to probe for the presence of lipid rafts; rafts here would be defined as membrane domains containing clustered GPI-anchored proteins at the cell surface. The results of these studies, each based on a single protein, gave conflicting views of rafts. To address the source of this discrepancy, we have now used FRET to study three different GPI-anchored proteins and a GSL endogenous to several different cell types. FRET was detected between molecules of the GSL GM1 labeled with cholera toxin B-subunit and between antibody-labeled GPI-anchored proteins, showing these raft markers are in submicrometer proximity in the plasma membrane. However, in most cases FRET correlated with the surface density of the lipid raft marker, a result inconsistent with significant clustering in microdomains. We conclude that in the plasma membrane, lipid rafts either exist only as transiently stabilized structures or, if stable, comprise at most a minor fraction of the cell surface.

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Section: Discussionmentioning

confidence: 65%

Section: Plasma Membrane Distribution Of Lipid Raft Markers Detected mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

High-Resolution FRET Microscopy of Cholera Toxin B-Subunit and GPI-anchored Proteins in Cell Plasma Membranes

Kenworthy

Petranova

Edidin

2000

MBoC

406

311

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“…Ordered regions of membrane, known as microdomains, lipid rafts, detergent-resistant membranes (DRMs), and other abbreviations are thought to be critical sites of signal propagation and membrane trafficking (Edidin, 1997(Edidin, , 2001Simons and Ikonen, 1997;Anderson, 1998;London, 1998, 2000;Jacobson and Dietrich, 1999;Langlet et al, 2000;Anderson and Jacobson, 2002). Analysis of these regions typically begins with detergent solubilization of whole cells followed by sucrose density gradient centrifugation and the recovery of detergent-resistant membranes from the light fractions of the gradient.…”

Section: Introductionmentioning

confidence: 99%

Markers for Detergent-resistant Lipid Rafts Occupy Distinct and Dynamic Domains in Native Membranes

Wilson

Steinberg

Liederman

et al. 2004

MBoC

187

183

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Lipid rafts isolated by detergent extraction and sucrose gradient fractionation from mast cells are enriched for the glycosylphosphatidylinositol-linked protein Thy-1, the ganglioside GM1, palmitoylated LAT, and cross-linked IgE receptors, Fc⑀RI. This study addresses the relationship of fractionation data to the organization of raft markers in native membranes. Immunogold labeling and electron microscopy shows there is little or no colocalization of the raft markers Thy-1, GM1, and LAT with each other or with Fc⑀RI on native membrane sheets prepared from unstimulated cells. External cross-linking of Thy-1 promotes coclustering of Thy-1 with LAT, but not with GM1. Thy-1 and LAT clusters occur on membrane regions without distinctive features. In contrast, external cross-linking of Fc⑀RI and GM1 causes their redistribution to electron-dense membrane patches independently of each other and of Thy-1. The distinctive patches that accumulate cross-linked Fc⑀RI and GM1 also accumulate osmium, a stain for unsaturated lipids, and are sites for coated vesicle budding. Electron microscopy reveals a more complex and dynamic topographical organization of membrane microdomains than is predicted by biochemical analysis of detergent-resistant membranes. INTRODUCTIONOrdered regions of membrane, known as microdomains, lipid rafts, detergent-resistant membranes (DRMs), and other abbreviations are thought to be critical sites of signal propagation and membrane trafficking (Edidin, 1997(Edidin, , 2001Simons and Ikonen, 1997;Anderson, 1998; London, 1998, 2000;Jacobson and Dietrich, 1999;Langlet et al., 2000;Anderson and Jacobson, 2002). Analysis of these regions typically begins with detergent solubilization of whole cells followed by sucrose density gradient centrifugation and the recovery of detergent-resistant membranes from the light fractions of the gradient. The DRMs are enriched for caveolin, glycosylphosphatidylinositol-linked (GPI-linked) proteins, glycosphingolipids, GM1 ganglioside, and cholesterol, suggesting that these components are associated in the liquid-ordered (l o ) phase of the lipid bilayer (Schroeder et al., 1994;Ahmed et al., 1997). The interpretation of gradient centrifugation experiments remains controversial. There is evidence that detergents may force associations between components that are not colocalized in intact cells (Mayor and Maxfield, 1995), and fractionation results are known to be dramatically altered by varying the concentration of Triton X-100 (Field et al., 1999;Parolini et al., 1999), by use of alternative detergents (Montixi et al., 1998;Surviladze et al., 1998) or by omission of detergent altogether (Ilangumaran et al., 1999;Harder and Kuhn, 2000;Surviladze et al., 2001). Methods to observe membrane segregation in situ have also generated controversy. Results based on light and fluorescence microscopy of proteins and lipids, including refinements of the established fluorescence recovery after photobleaching methods and new single particle tracking methods, have led some investigators to co...

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CD24

Altevogt¹,

Friederichs²

2002

Wiley Encyclopedia of Molecular Medicine

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Looking at lipid rafts?

Cited by 395 publications

References 32 publications

High-Resolution FRET Microscopy of Cholera Toxin B-Subunit and GPI-anchored Proteins in Cell Plasma Membranes

High-Resolution FRET Microscopy of Cholera Toxin B-Subunit and GPI-anchored Proteins in Cell Plasma Membranes

Markers for Detergent-resistant Lipid Rafts Occupy Distinct and Dynamic Domains in Native Membranes

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