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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Main Authors: Thibault Annaval, Rebekka Wild, Yoann Crétinon, Rabia Sadir, Romain R. Vivès, Hugues Lortat-Jacob
Format: Article
Language:English
Published: MDPI AG 2020-09-01
Series:Molecules
Subjects:
Online Access:https://www.mdpi.com/1420-3049/25/18/4215
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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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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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