Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 107, Issue 41, Pages 17633-17638Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1012424107
Keywords
ciliogenesis; epithelial polarity; Forssman glycosphingolipid; protein-lipid interactions; raft clustering
Categories
Funding
- European Union [LSHB-CT2007-037740]
- Federal Ministry of Education and Support BioChance Plus [0313827DFG]
- European Science Foundation Lipid-Protein Interactions in Membrane Organization
- German Research Council [83]
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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 head groups 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.
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