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

被引:216
作者
Lehle, Ludwig
Strahl, Sabine
Tanner, Widmar
机构
[1] Univ Regensburg, Lehrstuhl Zellbiol & Pflanzenphysiol, D-93053 Regensburg, Germany
[2] Heidelberg Univ, Abt Zellchem 5, Heidelberger Inst Pflanzenwissensch, D-69120 Heidelberg, Germany
关键词
congenital disorders of glycosylation; dolichol; glycosylation; protein modification; transferases;
D O I
10.1002/anie.200601645
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
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. © 2006 Wiley-VCH Verlag GmbH &. Co. KGaA.
引用
收藏
页码:6802 / 6818
页数:17
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