Trafficking of galectin-3 through endosomal organelles of polarized and non-polarized cells

In epithelial cells, the β-galactoside-binding lectin galectin-3 mediates the non-raft-dependent glycoprotein targeting to the apical membrane domain. In this study, we aimed to identify intracellular compartments involved in the trafficking of galectin-3. By studying fluorescent fusion proteins in...

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Bibliographic Details
Published in:European journal of cell biology 2010-11, Vol.89 (11), p.788-798
Main Authors: Schneider, Dominik, Greb, Christoph, Koch, Annett, Straube, Tamara, Elli, Alexandra, Delacour, Delphine, Jacob, Ralf
Format: Article
Language:English
Subjects:
Animals
Apical trafficking
Cell Line
Cell Membrane - metabolism
Cell Polarity - genetics
Cercopithecus aethiops
COS Cells
COS-1
Dogs
Endosomes
Endosomes - genetics
Endosomes - metabolism
Epithelial Cells - cytology
Epithelial Cells - metabolism
Galectin 3 - genetics
Galectin 3 - metabolism
Galectin-3
MDCK
Microscopy, Fluorescence
Organelles - genetics
Organelles - metabolism
Protein Transport
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Summary:In epithelial cells, the β-galactoside-binding lectin galectin-3 mediates the non-raft-dependent glycoprotein targeting to the apical membrane domain. In this study, we aimed to identify intracellular compartments involved in the trafficking of galectin-3. By studying fluorescent fusion proteins in living cells, we could show that galectin-3 accumulates intracellularly in acidified endosomes. Total internal reflection fluorescence microscopy studies of the apical surface of polarized MDCK cells revealed that galectin-3 is enriched in tubular and vesicular Rab11-positive recycling endosomes in the vicinity of the apical cell surface. These endosomal organelles are candidate compartments for the association between galectin-3 and exocytic apical cargo.
ISSN:0171-9335
1618-1298
DOI:10.1016/j.ejcb.2010.07.001