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Int. J. Mol. Sci. 2016, 17(10), 1732;

Glycosphingolipid–Protein Interaction in Signal Transduction

Institute of Protein Biochemistry National Research Council, Via P. Castellino 111, Naples 80131, Italy
Istituto di Ricovero e Cura a Carattere Scientifico SDN, Via Emanuele Gianturco 113, Naples 80143, Italy
Author to whom correspondence should be addressed.
Academic Editor: Cheorl-Ho Kim
Received: 29 July 2016 / Revised: 4 October 2016 / Accepted: 10 October 2016 / Published: 15 October 2016
(This article belongs to the Special Issue Glycan–Receptor Interaction)
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Glycosphingolipids (GSLs) are a class of ceramide-based glycolipids essential for embryo development in mammals. The synthesis of specific GSLs depends on the expression of distinctive sets of GSL synthesizing enzymes that is tightly regulated during development. Several reports have described how cell surface receptors can be kept in a resting state or activate alternative signalling events as a consequence of their interaction with GSLs. Specific GSLs, indeed, interface with specific protein domains that are found in signalling molecules and which act as GSL sensors to modify signalling responses. The regulation exerted by GSLs on signal transduction is orthogonal to the ligand–receptor axis, as it usually does not directly interfere with the ligand binding to receptors. Due to their properties of adjustable production and orthogonal action on receptors, GSLs add a new dimension to the control of the signalling in development. GSLs can, indeed, dynamically influence progenitor cell response to morphogenetic stimuli, resulting in alternative differentiation fates. Here, we review the available literature on GSL–protein interactions and their effects on cell signalling and development. View Full-Text
Keywords: glycosphingolipid; signalling; glycan–protein interaction glycosphingolipid; signalling; glycan–protein interaction

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Russo, D.; Parashuraman, S.; D’Angelo, G. Glycosphingolipid–Protein Interaction in Signal Transduction. Int. J. Mol. Sci. 2016, 17, 1732.

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