Abstract
Gangliosides, the glycosphingolipids carrying one or several sialic acid residues, are located on the outer leaflet of the plasma membrane in glycolipid-enriched microdomains, where they interact with molecules of signal transduction pathways including receptors tyrosine kinases (RTKs). The role of gangliosides in the regulation of signal transduction has been reported in many cases and in a large number of cell types. In this review, we summarize the current knowledge on the biosynthesis of gangliosides and the mechanism by which they regulate RTKs signaling.
Highlights
Gangliosides are glycosphingolipids (GSL) carrying one or several sialic acid residues
It is clear that gangliosides regulate receptors tyrosine kinases (RTKs) within glycolipid-enriched microdomains either by inhibiting the dimerization and autophosphorylation of the receptors induced by specific ligands, or activating receptors signaling without ligand binding
The activation or inhibition of RTKs is dependent on the glycan structure of gangliosides and cellular context
Summary
Gangliosides are glycosphingolipids (GSL) carrying one or several sialic acid residues. Amongst the membrane-bound proteins associated to GEMs, many components of signal transduction pathways were identified. The role of GEMs-associated gangliosides in the regulation of signal transduction has been repeatedly reported in a variety of cell lines [9,10,11]. Apprehending the structural heterogeneity and the diversity of interactions between gangliosides and the other components of GEMs should lead to a better understanding of the fine regulation of signal transduction. This has been eased by recent advances in structural analysis of GEMs glycolipids and by the identification of GEMs associated molecules, as reviewed
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