Strasser Richard
Department of Applied Genetics and Cell Biology, Institute of Plant Biotechnology and Cell Biology, University of Natural Resources and Life Sciences, Vienna, Austria.
Front Plant Sci. 2022 Apr 25;13:897549. doi: 10.3389/fpls.2022.897549. eCollection 2022.
Asparagine ()-linked protein glycosylation is a ubiquitous co- and posttranslational modification which has a huge impact on the biogenesis and function of proteins and consequently on the development, growth, and physiology of organisms. In mammals, -glycan processing carried out by Golgi-resident glycosidases and glycosyltransferases creates a number of structurally diverse -glycans with specific roles in many different biological processes. In plants, complex -glycan modifications like the attachment of β1,2-xylose, core α1,3-fucose, or the Lewis A-type structures are evolutionary highly conserved, but their biological function is poorly known. Here, I highlight recent developments that contribute to a better understanding of these conserved glycoprotein modifications and discuss future directions to move the field forward.
天冬酰胺(N)-连接的蛋白质糖基化是一种普遍存在的共翻译和翻译后修饰,对蛋白质的生物合成和功能有巨大影响,进而对生物体的发育、生长和生理过程产生影响。在哺乳动物中,由高尔基体驻留糖苷酶和糖基转移酶进行的N-聚糖加工产生了许多结构多样的N-聚糖,它们在许多不同的生物过程中具有特定作用。在植物中,复杂的N-聚糖修饰,如β1,2-木糖、核心α1,3-岩藻糖的附着或Lewis A型结构,在进化上高度保守,但其生物学功能却鲜为人知。在此,我重点介绍了有助于更好理解这些保守糖蛋白修饰的最新进展,并讨论了推动该领域向前发展的未来方向。