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 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.
Schneider
Dominik
D
Department of Cell Biology and Cell Pathology, Philipps-Universität Marburg, Marburg, Germany.
Greb
Christoph
C
Koch
Annett
A
Straube
Tamara
T
Elli
Alexandra
A
Delacour
Delphine
D
Jacob
Ralf
R
D000818:Animals; D019556:COS Cells; D002460:Cell Line; D002462:Cell Membrane / Q000378:metabolism; D016764:Cell Polarity / Q000235:genetics; D002522:Chlorocebus aethiops; D004285:Dogs; D011992:Endosomes / Q000235:genetics / Q000378:metabolism*; D004847:Epithelial Cells / Q000166:cytology / Q000378:metabolism; D037502:Galectin 3 / Q000235:genetics / Q000378:metabolism*; D008856:Microscopy, Fluorescence; D015388:Organelles / Q000235:genetics / Q000378:metabolism*; D021381:Protein Transport
D037502:Galectin 3