Microdomains of GPI-anchored proteins in living cells revealed by crosslinking

Tim Friedrichson and Teymuras V. Kurzchalia ()
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Tim Friedrichson: Max Delbrück Centre for Molecular Medicine
Teymuras V. Kurzchalia: Max Delbrück Centre for Molecular Medicine

Nature, 1998, vol. 394, issue 6695, 802-805

Abstract: Abstract There is some discussion as to whether glycosyl-phosphatidylinositol(GPI)-anchored proteins occur in microdomains in the cell membrane1,2. These putative microdomains have been implicated in processes such as sorting in polarized cells3,4,5 and signal transduction6,7,8. 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 proteins9,10. 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 state11,12,13. 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.

Date: 1998
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DOI: 10.1038/29570

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