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Updated: Feb 10, 2026

Complementation of Splicing Activity by a Galectin-3 - U1 snRNP Complex on Beads
Published on: December 9, 2020
Galectin-3 modulates the polarized surface delivery of β1-integrin in epithelial cells
Ellena Hönig1, Karina Ringer1,2, Jenny Dewes1
1Department of Cell Biology and Cell Pathology, Philipps-Universität Marburg, Marburg 35037, Germany.
Abstract:
Epithelial cells require a precise intracellular transport and sorting machinery to establish and maintain their polarized architecture. This machinery includes β-galactoside-binding galectins for targeting of glycoprotein to the apical membrane. Galectin-3 sorts cargo destined for the apical plasma membrane into vesicular carriers. After delivery of cargo to the apical milieu, galectin-3 recycles back into sorting organelles. We analysed the role of galectin-3 in the polarized distribution of β1-integrin in MDCK cells. Integrins are located primarily at the basolateral domain of epithelial cells. We demonstrate that a minor pool of β1-integrin interacts with galectin-3 at the apical plasma membrane. Knockdown of galectin-3 decreases apical delivery of β1-integrin. This loss is restored by supplementation with recombinant galectin-3 and galectin-3 overexpression. Our data suggest that galectin-3 targets newly synthesized β1-integrin to the apical membrane and promotes apical delivery of β1-integrin internalized from the basolateral membrane. In parallel, knockout of galectin-3 results in a reduction in cell proliferation and an impairment in proper cyst development. Our results suggest that galectin-3 modulates the surface distribution of β1-integrin and affects the morphogenesis of polarized cells.
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