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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Main Author: Erika Staudacher
Format: Article
Language:English
Published: MDPI AG 2015-06-01
Series:Molecules
Subjects:
Online Access:http://www.mdpi.com/1420-3049/20/6/10622
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author Erika Staudacher
author_facet Erika Staudacher
author_sort Erika Staudacher
collection DOAJ
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 doaj.art-90aa7bd3f72f4cb1a6bfffd41fdf45d82022-12-22T00:51:44ZengMDPI AGMolecules1420-30492015-06-01206106221064010.3390/molecules200610622molecules200610622Mucin-Type O-Glycosylation in InvertebratesErika Staudacher0Department of Chemistry, University of Natural Resources and Life Sciences, Vienna, Muthgasse 18, 1190 Vienna, AustriaO-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.http://www.mdpi.com/1420-3049/20/6/10622O-glycosylationinvertebratesmucin-typenematodeinsecthelminthmollusc
spellingShingle Erika Staudacher
Mucin-Type O-Glycosylation in Invertebrates
Molecules
O-glycosylation
invertebrates
mucin-type
nematode
insect
helminth
mollusc
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 O-glycosylation
invertebrates
mucin-type
nematode
insect
helminth
mollusc
url http://www.mdpi.com/1420-3049/20/6/10622
work_keys_str_mv AT erikastaudacher mucintypeoglycosylationininvertebrates