Dean N
Department of Biochemistry and Cell Biology, Institute for Cell and Developmental Biology, State University of New York, Stony Brook, NY 11794-5215, USA.
Biochim Biophys Acta. 1999 Jan 6;1426(2):309-22. doi: 10.1016/s0304-4165(98)00132-9.
The Golgi complex is the site where the terminal carbohydrate modification of proteins and lipids occurs. These carbohydrates play a variety of biological roles, ranging from the stabilization of glycoprotein structure to the provision of ligands for cell-cell interactions to the regulation of cell surface properties. Progress in our understanding of the biosynthesis and regulation of glycoconjugates has been accelerating at a rapid pace. Recent advances in the field of yeast glycobiology have been particularly impressive. This review focuses on glycosylation of proteins in the Golgi of the yeast Saccharomyces cerevisiae, with emphasis on the candidate mannosyltransferases that participate in the synthesis of N-linked oligosaccharides. Current views on how these enzymes may be regulated and how glycosylation relates on other cellular processes are also discussed.
高尔基体是蛋白质和脂质进行终末碳水化合物修饰的场所。这些碳水化合物发挥着多种生物学作用，从稳定糖蛋白结构到提供细胞间相互作用的配体，再到调节细胞表面特性。我们对糖缀合物生物合成和调控的理解一直在快速进展。酵母糖生物学领域的最新进展尤其令人瞩目。本综述聚焦于酿酒酵母高尔基体中蛋白质的糖基化，重点关注参与N - 连接寡糖合成的候选甘露糖基转移酶。还讨论了关于这些酶如何被调控以及糖基化与其他细胞过程如何关联的当前观点。
