Article Dans Une Revue American Journal of Physiology - Cell Physiology Année : 2022

The glycosaminoglycan interactome 2.0

Résumé

Glycosaminoglycans (GAGs) are complex linear polysaccharides, which are covalently attached to core proteins (except for hyaluronan) to form proteoglycans. They play key roles in the organization of the extracellular matrix, and at the cell surface where they contribute to the regulation of cell signaling and of cell adhesion. To explore the mechanisms and pathways underlying their functions, we have generated an expanded dataset of 4,290 interactions corresponding to 3,464 unique GAG-binding proteins, four times more than the first version of the GAG interactome (Vallet, Clerc, and Ricard-Blum. J Histochem Cytochem 69: 93–104, 2021). The increased size of the GAG network is mostly due to the addition of GAG-binding proteins captured from cell lysates and biological fluids by affinity chromatography and identified by mass spectrometry. We review here the interaction repertoire of natural GAGs and of synthetic sulfated hyaluronan, the specificity and molecular functions of GAG-binding proteins, and the biological processes and pathways they are involved in. This dataset is also used to investigate the differences between proteins binding to iduronic acid-containing GAGs (dermatan sulfate and heparin/heparan sulfate) and those interacting with GAGs lacking iduronic acid (chondroitin sulfate, hyaluronan, and keratan sulfate).

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Cite 10.6084/m9.figshare.c.5907695.v1 Article RICARD-BLUM, S. (2022). The glycosaminoglycan interactome 2.0. figshare. https://doi.org/10.6084/M9.FIGSHARE.C.5907695.V1

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hal-04871745 , version 1 (07-01-2025)

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Sylvain Vallet, Coline Berthollier, Sylvie Ricard-Blum. The glycosaminoglycan interactome 2.0. American Journal of Physiology - Cell Physiology, 2022, Deciphering the Role of Proteoglycans and Glycosaminoglycans in Health and Disease, 322 (6), pp.C1271-C1278. ⟨10.1152/ajpcell.00095.2022⟩. ⟨hal-04871745⟩
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