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Galectin-9 trafficking regulates apical-basal polarity in Madin-Darby canine kidney epithelial cells

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Mishra,  Rashmi
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

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Grzybek,  Michal
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

Niki,  Toshiro
Max Planck Society;

Hirashima,  Mitsuomi
Max Planck Society;

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Simons,  Kai
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

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Citation

Mishra, R., Grzybek, M., Niki, T., Hirashima, M., & Simons, K. (2010). Galectin-9 trafficking regulates apical-basal polarity in Madin-Darby canine kidney epithelial cells. Proceedings of the National Academy of Sciences of the United States of America, 107(41), 17633-17638.


Cite as: http://hdl.handle.net/21.11116/0000-0001-0B73-2
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.