Journal
MOLECULES
Volume 25, Issue 18, Pages -Publisher
MDPI
DOI: 10.3390/molecules25184215
Keywords
proteoglycan; glycosaminoglycan; heparan sulfate; glycosylation; biosynthesis; biosynthesis and post synthetic enzymes
Funding
- Agence Nationale de la Recherche [ANR-18-CE11-0006-01]
- Grenoble Alliance for Integrated Structural Cell Biology (GRAL) within the Grenoble Partnership for Structural Biology [ANR-10-LABX-49-01]
- Investissements d'avenir program Glyco@Alps [ANR-15-IDEX-02]
- ANR
- Agence Nationale de la Recherche (ANR) [ANR-18-CE11-0006] Funding Source: Agence Nationale de la Recherche (ANR)
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Glycosylation is a common and widespread post-translational modification that affects a large majority of proteins. Of these, a small minority, about 20, are specifically modified by the addition of heparan sulfate, a linear polysaccharide from the glycosaminoglycan family. The resulting molecules, heparan sulfate proteoglycans, nevertheless play a fundamental role in most biological functions by interacting with a myriad of proteins. This large functional repertoire stems from the ubiquitous presence of these molecules within the tissue and a tremendous structural variety of the heparan sulfate chains, generated through both biosynthesis and post synthesis mechanisms. The present review focusses on how proteoglycans are gagosylated and acquire structural complexity through the concerted action of Golgi-localized biosynthesis enzymes and extracellular modifying enzymes. It examines, in particular, the possibility that these enzymes form complexes of different modes of organization, leading to the synthesis of various oligosaccharide sequences.
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