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Updated: May 11, 2026

The Cell-based L-Glutathione Protection Assays to Study Endocytosis and Recycling of Plasma Membrane Proteins
Published on: December 13, 2013
pH-dependent recycling of galectin-3 at the apical membrane of epithelial cells
Tamara Straube1, Tobias von Mach, Ellena Hönig
1Department of Cell Biology and Cell Pathology, Philipps-Universität Marburg, D-35033, Marburg, Germany.
Abstract:
The β-galactoside binding protein galectin-3 is highly expressed in a variety of epithelial cell lines. Polarized MDCK cells secrete this lectin predominantly into the apical medium by non-classical secretion. Once within the apical extracellular milieu, galectin-3 can re-enter the cell followed by passage through endosomal organelles and modulate apical protein sorting. Here, we could show that galectin-3 is internalized by non-clathrin mediated endocytosis. Within endosomal organelles this pool associates with newly synthesized neurotrophin receptor in the biosynthetic pathway and assists in its membrane targeting. This recycling process is accompanied by transient interaction of galectin-3 with detergent insoluble membrane microdomains in a lactose- and pH-dependent manner. Moreover, in the presence of lactose, apical sorting of the neurotrophin receptor is affected following endosomal deacidification. Taken together, our results suggest that internalized galectin-3 directs the subcellular targeting of apical glycoproteins by membrane recycling.
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