(Q44037729)

29 November 2017

title

Alterations in membrane cholesterol that affect structure and function of caveolae (English)

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29 November 2017

Eric J Smart

1

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29 November 2017

Richard G W Anderson

series ordinal

2

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29 November 2017

language of work or name

English

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publication date

1 January 2002

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29 November 2017

published in

Methods in Enzymology

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29 November 2017

volume

353

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29 November 2017

page(s)

131-139

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Caveolin, a protein component of caveolae membrane coats

29 November 2017

cites work

1 reference

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Protein kinase C activators inhibit receptor-mediated potocytosis by preventing internalization of caveolae

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Dynamin-mediated internalization of caveolae.

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Dynamin at the neck of caveolae mediates their budding to form transport vesicles by GTP-driven fission from the plasma membrane of endothelium

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The caveolae membrane system

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Caveolins, liquid-ordered domains, and signal transduction

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Lowering the cholesterol content of MA104 cells inhibits receptor-mediated transport of folate

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Cholesterol controls the clustering of the glycophospholipid-anchored membrane receptor for 5-methyltetrahydrofolate

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Caveolin moves from caveolae to the Golgi apparatus in response to cholesterol oxidation

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The glycophospholipid-linked folate receptor internalizes folate without entering the clathrin-coated pit endocytic pathway

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Potocytosis: Sequestration and Transport of Small Molecules by Caveolae

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Acylation targets emdothelial nitric-oxide synthase to plasmalemmal caveolae

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High density lipoprotein prevents oxidized low density lipoprotein-induced inhibition of endothelial nitric-oxide synthase localization and activation in caveolae.

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Oxidized low density lipoprotein displaces endothelial nitric-oxide synthase (eNOS) from plasmalemmal caveolae and impairs eNOS activation

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Cholesterol depletion of caveolae causes hyperactivation of extracellular signal-related kinase (ERK).

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Characterization of a cytosolic heat-shock protein-caveolin chaperone complex. Involvement in cholesterol trafficking

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Palmitoylation of caveolin-1 is required for cholesterol binding, chaperone complex formation, and rapid transport of cholesterol to caveolae

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Identification of caveolin-1 in lipoprotein particles secreted by exocrine cells

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Src tyrosine kinases, Galpha subunits, and H-Ras share a common membrane-anchored scaffolding protein, caveolin. Caveolin binding negatively regulates the auto-activation of Src tyrosine kinases

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Identification of peptide and protein ligands for the caveolin-scaffolding domain. Implications for the interaction of caveolin with caveolae-associated proteins

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How do the polyene macrolide antibiotics affect the cellular membrane properties?

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Permeabilizing action of filipin III on model membranes through a filipin-phospholipid binding

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Polyene antibiotic-sterol interactions in membranes of Acholeplasma laidlawii cells and lecithin liposomes. 3. Molecular structure of the polyene antibiotic-cholesterol complexes

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Cholesterol oxidase: sources, physical properties and analytical applications

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Efflux of Cholesterol from Different Cellular Pools†

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Isolation and characterization of apolipoprotein B-100

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Microsomal lipid peroxidation

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7 January 2021

A role for caveolin in transport of cholesterol from endoplasmic reticulum to plasma membrane

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7 January 2021

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Identifiers

DOI

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29 November 2017

1 reference