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Science 24 June 1994: Vol. 264. no. 5167, pp. 1948 - 1951 DOI: 10.1126/science.7516582
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Articles
Science, Vol 264, Issue 5167, 1948-1951
Copyright © 1994 by American Association for the Advancement of Science
Sequestration of GPI-anchored proteins in caveolae triggered by cross-linking
S Mayor,
KG Rothberg,
and
FR Maxfield
Department of Pathology, College of Physicians and Surgeons, Columbia University, New York, NY 10032.
Glycosyl-phosphatidylinositol (GPI)-anchored proteins have been reported to reside in clusters collected over small membrane invaginations called caveolae. The detection of different GPI-anchored proteins with fluorescently labeled monoclonal antibodies showed that these proteins are not constitutively concentrated in caveolae; they enter these structures independently after cross-linking with polyclonal secondary antibodies. Analysis of the cell surface distribution of the GPI-anchored folate receptor by electron microscopy confirms these observations. Thus, multimerization of GPI-anchored proteins regulates their sequestration in caveolae, but in the absence of agents that promote clustering they are diffusely distributed over the plasma membrane.
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