Abstract
Membrane folate recepter (MFR) type 2 is one of the two isoforms originally identified in human placenta 1. In the rough Endoplasmic Reticulum MFR-2 is provided with N-linked oligosaccharide chains and a glycosyl phosphatidylinositol (GPI) membrane-anchor, which has been shown to serve as a signal for the targeting of proteins to the apical plasma membrane domain in epithelial cells2. It has been suggested that GPI-linked proteins are sorted in the Golgi complex into microdomains enriched in glycolipids and cholesterol which leads to directional transport to the apical domain3,4,5. Recently, it has been shown that newly synthesized GPI-linked proteins have less lateral mobility when they arrive at the plasma membrane as compared to GPI-linked proteins that were allready present at the cell surface, again suggesting clustering of GPI-linked proteins at the plasma membrane6.
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© 1993 Springer Science+Business Media New York
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Rijnboutt, S. et al. (1993). Detergent-Insolubility During the Biosynthesis of Membrane Folate Receptor-2. In: Ayling, J.E., Nair, M.G., Baugh, C.M. (eds) Chemistry and Biology of Pteridines and Folates. Advances in Experimental Medicine and Biology, vol 338. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-2960-6_159
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DOI: https://doi.org/10.1007/978-1-4615-2960-6_159
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