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Open AccessJournal ArticleDOI

Uncoupling of the Cholera Toxin-GM1 Ganglioside Receptor Complex from Endocytosis, Retrograde Golgi Trafficking, and Downstream Signal Transduction by Depletion of Membrane Cholesterol

Anne A. Wolf, +2 more
- 03 May 2002 - 
- Vol. 277, Iss: 18, pp 16249-16256
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TLDR
It is found that endocytosis and trafficking of CT into the Golgi apparatus depended on membrane cholesterol, which implies that cholesterol may function to couple the CT-GM1 complex with raft domains and with other membrane components of the lipid raft required for CT entry into the cell.
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This article is published in Journal of Biological Chemistry.The article was published on 2002-05-03 and is currently open access. It has received 119 citations till now. The article focuses on the topics: Lipid raft & Secretory pathway.

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Citations
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Journal ArticleDOI

Caveolae/raft-dependent endocytosis.

TL;DR: It is proposed that caveolae and rafts are internalized via a common pathway, Caveolae/raft-dependent endocytosis, defined by its clathrin independence, dynamin dependence, and sensitivity to cholesterol depletion.
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Caveosomes and endocytosis of lipid rafts

TL;DR: It is now apparent that caveolin 1, one of the characteristic protein components of caveolae, might in fact act to slow or inhibit endocytosis, and it is likely that there are mechanisms that allow recruitment and targeting of specific molecules to caveosomes.
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Gangliosides are receptors for murine polyoma virus and SV40.

TL;DR: It is demonstrated that specific gangliosides can serve as plasma membrane receptors for these viruses, GD1a and GT1b for Py and GM1 for SV40, and binding and flotation assays were used to show that addition of these gangLiosides to phospholipid vesicles allowed specific binding of the respective viruses.

GM3-enriched microdomain involved in cell adhesion and signal transduction through carbohydrate-carbohydrate interaction in mouse melanoma B16 cells; Separation of'glycosphingolipid signaling domain' from caveolin- containing membrane fraction in mouse melanoma B16 cells and its role in cell adhesion coupled with signaling

TL;DR: The GM3-enriched subfractions, involved in cell adhesion and capable of sending signals through GM3, represents a membrane domain distinguishable from caveolin-containing subfraction or caveolae, and is hereby termed the “glycosphingolipid signaling domain” or ‘glycosignaling domain’.
Journal ArticleDOI

The intracellular voyage of cholera toxin: going retro.

TL;DR: Cholera toxin and related AB(5)-subunit toxins move from the plasma membrane through the trans-Golgi and endoplasmic reticulum (ER) to the cytosol of host cells, exploiting a specific glycolipid pathway rather than a protein pathway.
References
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Journal ArticleDOI

Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface

TL;DR: It is shown that a protein with a glycosylphosphatidyl inositol (GPI) anchor can be recovered from lysates of epithelial cells in a low density, detergent-insoluble form, supporting the model proposed by Simons and colleagues for sorting of certain membrane proteins to the apical surface after intracellular association with glycosphingolipids.
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How Cells Handle Cholesterol

TL;DR: The regulation of cholesterol homeostasis is now receiving a new focus, and this changed perspective may throw light on diseases caused by cholesterol excess, the prime example being atherosclerosis.
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Extraction of Cholesterol with Methyl-β-Cyclodextrin Perturbs Formation of Clathrin-coated Endocytic Vesicles

TL;DR: The results indicate that although clathrin-independent (and caveolae-independent) endocytosis still operates after removal of cholesterol, cholesterol is essential for the formation of clathin-coated endocytic vesicles.
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Structure and origin of ordered lipid domains in biological membranes

TL;DR: Evidence that one type of microdomain may exist in cell membranes is summarized, consisting of membrane fragments that are insoluble in cold non-ionic detergents such as Triton X-100, which may provide some of the first evidence for phase separation in biological membranes.
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Filipin-sensitive caveolae-mediated transport in endothelium: reduced transcytosis, scavenger endocytosis, and capillary permeability of select macromolecules.

TL;DR: It is shown that the ability of sterol binding agents such as filipin to disassemble endothelial noncoated but not coated plasmalemmal vesicles selectively inhibits caveolae-mediated intracellular and transcellular transport of select macromolecules in endothelium.
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