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Segregation of Heterologous GPI-Anchored Proteins Into Separate Membrane Rafts

Published online by Cambridge University Press:  02 July 2020

M. Ratnam ,
W. Gunning  and
J. Wang
M. Ratnam
Affiliation:
Department of Biochemistry & Molecular Biology, Medical College of Ohio, Toledo, OH , 43614
W. Gunning
Affiliation:
Department of Pathology, Medical College of Ohio, Toledo, OH , 43614
J. Wang
Affiliation:
Department of Biochemistry & Molecular Biology, Medical College of Ohio, Toledo, OH , 43614
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Abstract

Specific lipid self-associations in the fluid bilayer, particularly involving sphingolipids and cholesterol, are believed to result in the formation of membrane microdomains or “rafts” that mediate recycling of proteins between the cell surface and intracellular compartments or function as platforms for signal transduction events. Such membrane microdomains may be recovered in a low-density fraction that is insoluble in Triton X-100 at 4°C and referred to as detergent-insoluble, glycolipid-enriched complexes (DIGs). Membrane microdomains that constitute cell surface invaginations called caveolae can also be recovered in the form of DIGs. Caveolae are typically associated with a protein called caveolin, which coats their cytoplasmic surface.

Various glycosyl-phosphatidylinositol (GPI)-anchored proteins such as the folate receptor (FR) are believed to be associated with membrane rafts and to constitutively internalize and recycle to the cell surface although FR is the only known GPI-anchored protein with a transport function, i.e.,

Type
The Cell Biology of Cancer (Organized by J. Jerome and B. Gunning)
Information
Microscopy and Microanalysis , Volume 7 , Issue S2: Proceedings: Microscopy & Microanalysis 2001, Microscopy Society of America 59th Annual Meeting, Microbeam Analysis Society 35th Annual Meeting, Long Beach, California August 5-9, 2001 , August 2001 , pp. 584 - 585
Copyright
Copyright © Microscopy Society of America 2001

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