Dünser Kai, Schoberer Jennifer
Department of Biotechnology and Food Science, Institute of Plant Biotechnology and Cell Biology, BOKU University, Vienna, Austria.
Front Plant Sci. 2025 Jul 25;16:1624949. doi: 10.3389/fpls.2025.1624949. eCollection 2025.
Asparagine ()-linked glycosylation is a fundamental co- and post-translational modification of proteins, playing a crucial role in protein folding, stability and function, protein-protein interactions, biotic and abiotic stress response as well as glycan-dependent quality control processes in the endoplasmic reticulum (ER). Protein -glycosylation is initiated in the ER and continued in the Golgi apparatus by -glycan-processing glycosyltransferases and glycosidases, which are compartmentalized in a highly organized manner reflecting their function in the sequential modification of glycans. Therefore, the precise localization of these enzymes is crucial for the optimal functioning of the glycosylation process and the secretory pathway and hence must be tightly regulated to maintain protein function, cellular health, and overall organismal development. Here, we highlight recent developments that contribute to a better understanding of the localization mechanisms of this important class of Golgi residents and discuss future directions to move the field forward.
天冬酰胺（N）-连接糖基化是蛋白质一种基本的共翻译和翻译后修饰，在蛋白质折叠、稳定性和功能、蛋白质-蛋白质相互作用、生物和非生物胁迫响应以及内质网（ER）中依赖聚糖的质量控制过程中发挥着关键作用。蛋白质N-糖基化起始于内质网，并在高尔基体中由N-聚糖加工糖基转移酶和糖苷酶继续进行，这些酶以高度有组织的方式进行区室化，反映了它们在聚糖顺序修饰中的功能。因此，这些酶的精确定位对于糖基化过程和分泌途径的最佳功能至关重要，因此必须进行严格调控以维持蛋白质功能、细胞健康和整体生物体发育。在这里，我们重点介绍了有助于更好理解这类重要高尔基体驻留蛋白定位机制的最新进展，并讨论了推动该领域向前发展的未来方向。
