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Mucin-Type O-Glycosylation in Invertebrates

O-Glycosylation is one of the most important posttranslational modifications of proteins. It takes part in protein conformation, protein sorting, developmental processes and the modulation of enzymatic activities. In vertebrates, the basics of the biosynthetic pathway of O-glycans are already well u...

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Autor principal: Staudacher, Erika
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6272458/
https://www.ncbi.nlm.nih.gov/pubmed/26065637
http://dx.doi.org/10.3390/molecules200610622
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author Staudacher, Erika
author_facet Staudacher, Erika
author_sort Staudacher, Erika
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description O-Glycosylation is one of the most important posttranslational modifications of proteins. It takes part in protein conformation, protein sorting, developmental processes and the modulation of enzymatic activities. In vertebrates, the basics of the biosynthetic pathway of O-glycans are already well understood. However, the regulation of the processes and the molecular aspects of defects, especially in correlation with cancer or developmental abnormalities, are still under investigation. The knowledge of the correlating invertebrate systems and evolutionary aspects of these highly conserved biosynthetic events may help improve the understanding of the regulatory factors of this pathway. Invertebrates display a broad spectrum of glycosylation varieties, providing an enormous potential for glycan modifications which may be used for the design of new pharmaceutically active substances. Here, overviews of the present knowledge of invertebrate mucin-type O-glycan structures and the currently identified enzymes responsible for the biosynthesis of these oligosaccharides are presented, and the few data dealing with functional aspects of O-glycans are summarised.
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spelling pubmed-62724582018-12-31 Mucin-Type O-Glycosylation in Invertebrates Staudacher, Erika Molecules Review O-Glycosylation is one of the most important posttranslational modifications of proteins. It takes part in protein conformation, protein sorting, developmental processes and the modulation of enzymatic activities. In vertebrates, the basics of the biosynthetic pathway of O-glycans are already well understood. However, the regulation of the processes and the molecular aspects of defects, especially in correlation with cancer or developmental abnormalities, are still under investigation. The knowledge of the correlating invertebrate systems and evolutionary aspects of these highly conserved biosynthetic events may help improve the understanding of the regulatory factors of this pathway. Invertebrates display a broad spectrum of glycosylation varieties, providing an enormous potential for glycan modifications which may be used for the design of new pharmaceutically active substances. Here, overviews of the present knowledge of invertebrate mucin-type O-glycan structures and the currently identified enzymes responsible for the biosynthesis of these oligosaccharides are presented, and the few data dealing with functional aspects of O-glycans are summarised. MDPI 2015-06-09 /pmc/articles/PMC6272458/ /pubmed/26065637 http://dx.doi.org/10.3390/molecules200610622 Text en © 2015 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Staudacher, Erika
Mucin-Type O-Glycosylation in Invertebrates
title Mucin-Type O-Glycosylation in Invertebrates
title_full Mucin-Type O-Glycosylation in Invertebrates
title_fullStr Mucin-Type O-Glycosylation in Invertebrates
title_full_unstemmed Mucin-Type O-Glycosylation in Invertebrates
title_short Mucin-Type O-Glycosylation in Invertebrates
title_sort mucin-type o-glycosylation in invertebrates
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6272458/
https://www.ncbi.nlm.nih.gov/pubmed/26065637
http://dx.doi.org/10.3390/molecules200610622
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