Separation of caveolae from associated microdomains of GPI-anchored proteins
@article{Schnitzer1995SeparationOC,
title={Separation of caveolae from associated microdomains of GPI-anchored proteins},
author={Jenniffer Aparecida Schnitzer and DP McIntosh and Amanda Dvorak and J Liu and Phil Oh},
journal={Science},
year={1995},
volume={269},
pages={1435 - 1439}
}In situ coating of the surface of endothelial cells in rat lung with cationic colloidal silica particles was used to separate caveolae from detergent-insoluble membranes rich in glycosyl phosphatidylinositol (GPI)-anchored proteins but devoid of caveolin. Immunogold electron microscopy showed that ganglioside GM1-enriched caveolae associated with an annular plasmalemmal domain enriched in GPI-anchored proteins. The purified caveolae contained molecular components required for regulated…
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References
SHOWING 1-10 OF 67 REFERENCES
Sequestration of GPI-anchored proteins in caveolae triggered by cross-linking.
- BiologyScience
- 1994
Analysis of the cell surface distribution of the GPI-anchored folate receptor by electron microscopy confirms that multimerization regulates their sequestration in caveolae, but in the absence of agents that promote clustering they are diffusely distributed over the plasma membrane.
Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface
- BiologyCell
- 1992
Detergent-insoluble glycolipid microdomains in lymphocytes in the absence of caveolae.
- BiologyThe Journal of biological chemistry
- 1994
Signal transducing molecules and glycosyl-phosphatidylinositol-linked proteins form a caveolin-rich insoluble complex in MDCK cells
- BiologyThe Journal of cell biology
- 1993
It is proposed that caveolin could function as a transmembrane adaptor molecule that couples luminal G PI-linked proteins with cytoplasmically oriented signaling molecules during GPI- Membrane trafficking or GPI -mediated signal transduction events.
Glycolipid-anchored proteins in neuroblastoma cells form detergent- resistant complexes without caveolin
- BiologyThe Journal of cell biology
- 1995
It is reported here that the complexes prepared from N2a cells display the large size and low buoyant density characteristic of complexes isolated from sources that are rich in caveolae, and contain the same major constituents, including multiple GPI-anchored proteins, alpha and beta subunits of heterotrimeric G proteins, and the tyrosine kinases.
Caveolin forms a hetero-oligomeric protein complex that interacts with an apical GPI-linked protein: implications for the biogenesis of caveolae
- BiologyThe Journal of cell biology
- 1993
Using transfected MDCK cells as a model system, a complex of cell surface molecules that interact in a pH- and cholesterol-dependent fashion with an apical recombinant GPI-linked protein is identified and suggests that caveolae may assemble intracellularly during transport to the cell surface.
Caveolae from luminal plasmalemma of rat lung endothelium: microdomains enriched in caveolin, Ca(2+)-ATPase, and inositol trisphosphate receptor.
- BiologyProceedings of the National Academy of Sciences of the United States of America
- 1995
To delineate the transport role of caveolae, they were purified from isolated luminal endothelial plasma membranes of rat lung and contained the plasmalemmal Ca(2+)-ATPase and inositol 1,4,5-trisphosphate surface receptors.
GPI-anchored proteins associate to form microdomains during their intracellular transport in Caco-2 cells.
- BiologyJournal of cell science
- 1993
The data suggest that GPI-anchored proteins cluster to form membrane microdomains together with an apical transmembrane protein, providing a possible apical sorting mechanism for intestinal cells in vitro that might be related to apicals sorting in MDCK cells, and that other mechanisms might exist to sort proteins to the apical membrane.
Purification and characterization of smooth muscle cell caveolae
- BiologyThe Journal of cell biology
- 1994
A biochemical method for purifying caveolae from chicken smooth muscle cells is developed to better understand the molecular composition of this membrane specialization that mediates transcytosis across endothelial cells and the uptake of small molecules and ions by both epithelial and connective tissue cells.