Galectin-9 trafficking regulates apical-basal polarity in Madin–Darby canine kidney epithelial cells
Open Access
- 22 September 2010
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences of the United States of America
- Vol. 107 (41), 17633-17638
- https://doi.org/10.1073/pnas.1012424107
Abstract
Galectins are unconventionally secreted lectins that participate in the formation of glycoprotein lattices that perform a variety of cell surface functions. Galectins also bind glycosphingolipid headgroups with as yet unclear implications for cellular physiology. We report a specific interaction between galectin-9 and the Forssman glycosphingolipid (FGL) that is important for polarizing Madin–Darby canine kidney epithelial cells. Galectin-9 knockdown leads to a severe loss of epithelial polarity that can be rescued by addition of the recombinant protein. The FGL glycan is identified as the surface receptor that cycles galectin-9 to the Golgi apparatus from which the protein is recycled back to the apical surface. Together our results suggest a model wherein such glycosphingolipid–galectin couples form a circuit between the Golgi apparatus and the cell surface that in an epithelial context facilitates the apical sorting of proteins and lipids.This publication has 34 references indexed in Scilit:
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