Protein glycosylation, conserved from yeast to man: a model organism helps elucidate congenital human diseases

Proteins can be modified by a large variety of covalently linked saccharides. The present review concentrates on two types, protein N-glycosylation and protein O-mannosylation, which, with only a few exceptions, are evolutionary conserved from yeast to man. They are also distinguished by some specia...

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Hauptverfasser: Lehle, Ludwig (VerfasserIn) , Strahl, Sabine (VerfasserIn) , Tanner, Widmar (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: 6 October 2006
In: Angewandte Chemie. International edition
Year: 2006, Jahrgang: 45, Heft: 41, Pages: 6802-6818
ISSN:1521-3773
DOI:10.1002/anie.200601645
Online-Zugang:Verlag, Volltext: http://dx.doi.org/10.1002/anie.200601645
Verlag, Volltext: http://onlinelibrary.wiley.com/doi/10.1002/anie.200601645/abstract
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Verfasserangaben:Ludwig Lehle, Sabine Strahl, and Widmar Tanner
Beschreibung
Zusammenfassung:Proteins can be modified by a large variety of covalently linked saccharides. The present review concentrates on two types, protein N-glycosylation and protein O-mannosylation, which, with only a few exceptions, are evolutionary conserved from yeast to man. They are also distinguished by some special features: The corresponding glycosylation processes start in the endoplasmatic reticulum, are continued in the Golgi apparatus, and require dolichol-activated precursors for the initial biosynthetic steps. With respect to the molecular biology of both types of protein glycosylation, the pathways and the genetic background of the reactions have most successfully been studied with the genetically easy-to-handle baker's yeast, Saccharomyces cerevisae. Many of the severe developmental disturbances in children are related to protein glycosylation, for example, the CDG syndrome (congenital disorders of glycosylation) as well as congenital muscular dystrophies with neuronal-cell-migration defects have been elucidated with the help of yeast.
Beschreibung:Dedicated to Professor Kandler on the occasion of his 85th birthday
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Beschreibung:Online Resource
ISSN:1521-3773
DOI:10.1002/anie.200601645