Galectin–glycan lattices regulate cell-surface glycoprotein organization and signalling
- 19 November 2008
- journal article
- review article
- Published by Portland Press Ltd. in Biochemical Society Transactions
- Vol. 36 (6) , 1472-1477
- https://doi.org/10.1042/bst0361472
Abstract
The formation of multivalent complexes of soluble galectins with glycoprotein receptors on the plasma membrane helps to organize glycoprotein assemblies on the surface of the cell. In some cell types, this formation of galectin–glycan lattices or scaffolds is critical for organizing plasma membrane domains, such as lipid rafts, or for targeted delivery of glycoproteins to the apical or basolateral surface. Galectin–glycan lattice formation is also involved in regulating the signalling threshold of some cell-surface glycoproteins, including T-cell receptors and growth factor receptors. Finally, galectin–glycan lattices can determine receptor residency time by inhibiting endocytosis of glycoprotein receptors from the cell surface, thus modulating the magnitude or duration of signalling from the cell surface. This paper reviews recent evidence in vitro and in vivo for critical physiological and cellular functions that are regulated by galectin–glycoprotein interactions.Keywords
This publication has 52 references indexed in Scilit:
- Removal of sialic acid involving Klotho causes cell-surface retention of TRPV5 channel via binding to galectin-1Proceedings of the National Academy of Sciences, 2008
- Endogenous galectin-1 enforces class I–restricted TCR functional fate decisions in thymocytesBlood, 2008
- Unconventional secretion of fibroblast growth factor 2 and galectin‐1 does not require shedding of plasma membrane‐derived vesiclesFEBS Letters, 2008
- Plasma membrane domain organization regulates EGFR signaling in tumor cellsThe Journal of cell biology, 2007
- Presentation of Galectin-1 by Extracellular Matrix Triggers T Cell DeathJournal of Biological Chemistry, 2004
- Specific Recognition of Leishmania major Poly-β-galactosyl Epitopes by Galectin-9Journal of Biological Chemistry, 2003
- The EGFR family and its ligands in human cancerEuropean Journal Of Cancer, 2001
- Expression of a Specific Glycosyltransferase Enzyme Regulates T Cell Death Mediated by Galectin-1Journal of Biological Chemistry, 2000
- Apoptosis of T cells mediated by galectin-1Nature, 1995
- The role of N‐glycosylation in the targeting and stability of GLUT1 glucose transporterFEBS Letters, 1993