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| Item Type: | Article |
|---|---|
| Title: | Microdomains of GPI-anchored proteins in living cells revealed by crosslinking |
| Creators Name: | Friedrichson, T. and Kurzchalia, T.V. |
| Abstract: | There is some discussion as to whether glycosyl-phosphatidylinositol(GPI)-anchored proteins occur in microdomains in the cell membrane. These putative microdomains have been implicated in processes such as sorting in polarized cells and signal transduction. Complexes enriched in GPI-anchored proteins, cholesterol and glycosphingolipids have been isolated from cell membranes by using non-ionic detergents: these complexes were thought to represent a clustered arrangement of GPI-anchored proteins. However, results obtained when clustering of GPI-anchored proteins induced by antibodies or by detergents was prevented support the idea of a dispersed surface distribution of GPI-anchored proteins at steady state. Here we use chemical crosslinking to show that membrane microdomains of a GPI-anchored protein exist at the surface in living cells. This clustering is specific for the GPI-anchored form, as two transmembrane forms bearing the same ectodomain do not form oligomers. Depletion of membrane cholesterol causes the clustering of GPI-anchored proteins to break up, whereas treatment of cells with detergent substantially increases the size of the complexes. We find that in living cells these GPI-anchored proteins reside in microdomains consisting of at least 15 molecules, which are much smaller than those seen after detergent extraction. |
| Keywords: | CD55 Antigens, CHO Cells, Cell Line, Cell Membrane, Cross-Linking Reagents, Detergents, Glycosylphosphatidylinositols, Growth Hormone, Molecular Cloning, Animals, Cricetinae, Rats |
| Source: | Nature |
| ISSN: | 0028-0836 |
| Publisher: | Nature Publishing Group |
| Volume: | 394 |
| Number: | 6695 |
| Page Range: | 802-805 |
| Date: | 20 August 1998 |
| Official Publication: | https://doi.org/10.1038/29570 |
| PubMed: | View item in PubMed |
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