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The Journal of Cell Biology, Vol 110, 637-649, Copyright © 1990 by The Rockefeller University Press


ARTICLES

The glycophospholipid-linked folate receptor internalizes folate without entering the clathrin-coated pit endocytic pathway

KG Rothberg, YS Ying, JF Kolhouse, BA Kamen and RG Anderson
Department of Cell Biology and Neuroscience, University of Texas Southwestern Medical Center, Dallas 75235.

The folate receptor, also known as the membrane folate-binding protein, is maximally expressed on the surface of folate-depleted tissue culture cells and mediates the high affinity accumulation of 5- methyltetrahydrofolic acid in the cytoplasm of these cells. Recent evidence suggests that this receptor recycles during folate internalization and that it is anchored in the membrane by a glycosyl- phosphatidylinositol linkage. Using quantitative immunocytochemistry, we now show that (a) this receptor is highly clustered on the cell surface; (b) these clusters are preferentially associated with uncoated membrane invaginations rather than clathrin-coated pits; and (c) the receptor is not present in endosomes or lysosomes. This receptor appears to physically move in and out of the cell using a novel uncoated pit pathway that does not merge with the clathrin-coated pit endocytic machinery.
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