Developmental Glycobiology Section, NIDCR, National Institutes of Health, Building 30, Room 426, 30 Convent Drive, MSC 4370, Bethesda, MD 20892-4370, United States.
Developmental Glycobiology Section, NIDCR, National Institutes of Health, Building 30, Room 426, 30 Convent Drive, MSC 4370, Bethesda, MD 20892-4370, United States.
Curr Opin Struct Biol. 2019 Jun;56:139-145. doi: 10.1016/j.sbi.2019.01.014. Epub 2019 Mar 7.
Glycosylation, or the addition of sugars to proteins, is a highly conserved protein modification defined by both the monosaccharide initially added as well as the amino acid to which it is attached. O-Linked glycosylation represents a diverse group of protein modifications occurring on the hydroxyl groups of serine and/or threonine residues. O-Glycosylation can have wide-ranging effects on protein stability and function, which translate into crucial consequences at the organismal level. This review will summarize structural and biological insights into the major O-glycans formed within the secretory apparatus (O-GalNAc, O-Man, O-Fuc, O-Glc and extracellular O-GlcNAc) from studies in the fruit fly Drosophila melanogaster. Drosophila has many advantages for investigating these complex modifications, boasting reduced functional redundancy within gene families, reduced length/complexity of glycan chains and sophisticated genetic tools. Gaining an understanding of the normal cellular and developmental roles of these conserved modifications in Drosophila will provide insight into how changes in O-glycans are involved in human disease and disease susceptibilities.
糖基化，即糖链添加到蛋白质上，是一种高度保守的蛋白质修饰，其定义既包括最初添加的单糖，也包括与其连接的氨基酸。O-连接糖基化是一类广泛存在的蛋白质修饰，发生在丝氨酸和/或苏氨酸残基的羟基上。O-糖基化对蛋白质稳定性和功能有广泛的影响，进而在机体水平上产生重要的后果。这篇综述将总结从果蝇（Drosophila melanogaster）研究中获得的关于在分泌装置中形成的主要 O-聚糖（O-GalNAc、O-Man、O-Fuc、O-Glc 和细胞外 O-GlcNAc）的结构和生物学见解。果蝇具有许多优势，可用于研究这些复杂的修饰，其基因家族的功能冗余较少，聚糖链的长度/复杂性降低，并且具有复杂的遗传工具。了解这些保守修饰在果蝇中的正常细胞和发育作用，将有助于深入了解 O-聚糖的变化如何参与人类疾病和疾病易感性。
