Sequestration of GPI-Anchored Proteins in Caveolae Triggered by Cross-Linking

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 constitutiv...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 1994-06, Vol.264 (5167), p.1948-1951
Main Authors: Mayor, Satyajit, Rothberg, Karen G., Maxfield, Frederick R.
Format: Article
Language:English
Subjects:
3T3 Cells
Animals
Antibodies
Antibodies, Monoclonal
Antigens, CD - analysis
Antigens, CD - immunology
Antigens, CD - metabolism
Antigens, Surface - analysis
Antigens, Surface - immunology
Antigens, Surface - metabolism
Biological and medical sciences
Caco 2 cells
Carrier Proteins - analysis
Carrier Proteins - immunology
Carrier Proteins - metabolism
Caveolae
Caveolin 1
Caveolins
CD55 Antigens
Cell coat. Cell surface
Cell lines
Cell Membrane - metabolism
Cell Membrane - ultrastructure
Cell membranes
Cell structures and functions
Cell surface receptors
Electron microscopy
Fluorescence
Fluorescent Antibody Technique
Folate Receptors, GPI-Anchored
Folic Acid - metabolism
Fundamental and applied biological sciences. Psychology
Glycosylphosphatidylinositols - analysis
Glycosylphosphatidylinositols - metabolism
Humans
Immunoglobulin G - metabolism
Membrane Glycoproteins - analysis
Membrane Glycoproteins - immunology
Membrane Glycoproteins - metabolism
Membrane Proteins - analysis
Mice
Microscopy, Electron
Molecular and cellular biology
Receptors
Receptors, Cell Surface
Room temperature
Sequestration (Chemistry)
Thy-1 Antigens
Tumor Cells, Cultured
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Description
Summary: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.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.7516582