Heparan Sulfate Proteoglycans Biosynthesis and Post Synthesis Mechanisms Combine Few Enzymes and Few Core Proteins to Generate Extensive Structural and Functional Diversity
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,...
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MDPI AG
2020-09-01
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author | Thibault Annaval Rebekka Wild Yoann Crétinon Rabia Sadir Romain R. Vivès Hugues Lortat-Jacob |
author_facet | Thibault Annaval Rebekka Wild Yoann Crétinon Rabia Sadir Romain R. Vivès Hugues Lortat-Jacob |
author_sort | Thibault Annaval |
collection | DOAJ |
description | 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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issn | 1420-3049 |
language | English |
last_indexed | 2024-03-10T16:20:41Z |
publishDate | 2020-09-01 |
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series | Molecules |
spelling | doaj.art-865e2942ae744b36a10dc57dc5c1e0f82023-11-20T13:42:42ZengMDPI AGMolecules1420-30492020-09-012518421510.3390/molecules25184215Heparan Sulfate Proteoglycans Biosynthesis and Post Synthesis Mechanisms Combine Few Enzymes and Few Core Proteins to Generate Extensive Structural and Functional DiversityThibault Annaval0Rebekka Wild1Yoann Crétinon2Rabia Sadir3Romain R. Vivès4Hugues Lortat-Jacob5Institut de Biologie Structurale, UMR 5075, University Grenoble Alpes, CNRS, CEA, 38000 Grenoble, FranceInstitut de Biologie Structurale, UMR 5075, University Grenoble Alpes, CNRS, CEA, 38000 Grenoble, FranceInstitut de Biologie Structurale, UMR 5075, University Grenoble Alpes, CNRS, CEA, 38000 Grenoble, FranceInstitut de Biologie Structurale, UMR 5075, University Grenoble Alpes, CNRS, CEA, 38000 Grenoble, FranceInstitut de Biologie Structurale, UMR 5075, University Grenoble Alpes, CNRS, CEA, 38000 Grenoble, FranceInstitut de Biologie Structurale, UMR 5075, University Grenoble Alpes, CNRS, CEA, 38000 Grenoble, FranceGlycosylation 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.https://www.mdpi.com/1420-3049/25/18/4215proteoglycanglycosaminoglycanheparan sulfateglycosylationbiosynthesisbiosynthesis and post synthetic enzymes |
spellingShingle | Thibault Annaval Rebekka Wild Yoann Crétinon Rabia Sadir Romain R. Vivès Hugues Lortat-Jacob Heparan Sulfate Proteoglycans Biosynthesis and Post Synthesis Mechanisms Combine Few Enzymes and Few Core Proteins to Generate Extensive Structural and Functional Diversity Molecules proteoglycan glycosaminoglycan heparan sulfate glycosylation biosynthesis biosynthesis and post synthetic enzymes |
title | Heparan Sulfate Proteoglycans Biosynthesis and Post Synthesis Mechanisms Combine Few Enzymes and Few Core Proteins to Generate Extensive Structural and Functional Diversity |
title_full | Heparan Sulfate Proteoglycans Biosynthesis and Post Synthesis Mechanisms Combine Few Enzymes and Few Core Proteins to Generate Extensive Structural and Functional Diversity |
title_fullStr | Heparan Sulfate Proteoglycans Biosynthesis and Post Synthesis Mechanisms Combine Few Enzymes and Few Core Proteins to Generate Extensive Structural and Functional Diversity |
title_full_unstemmed | Heparan Sulfate Proteoglycans Biosynthesis and Post Synthesis Mechanisms Combine Few Enzymes and Few Core Proteins to Generate Extensive Structural and Functional Diversity |
title_short | Heparan Sulfate Proteoglycans Biosynthesis and Post Synthesis Mechanisms Combine Few Enzymes and Few Core Proteins to Generate Extensive Structural and Functional Diversity |
title_sort | heparan sulfate proteoglycans biosynthesis and post synthesis mechanisms combine few enzymes and few core proteins to generate extensive structural and functional diversity |
topic | proteoglycan glycosaminoglycan heparan sulfate glycosylation biosynthesis biosynthesis and post synthetic enzymes |
url | https://www.mdpi.com/1420-3049/25/18/4215 |
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