Abstract：
The Golgi apparatus, a crucial organelle involved in protein processing, including glycosylation, exhibits complex sub-structures, i.e., cis-, medial, and trans-cisternae. This study investigated the distribution of glycosyltransferases within the Golgi apparatus of mammalian cells via 3D super-resolution imaging. Focusing on human glycosyltransferases involved in N-glycan modification, we found that even enzymes presumed to coexist in the same Golgi compartment exhibit nuanced variations in localization. By artificially making their N-terminal regions [composed of a cytoplasmic, transmembrane, and stem segment (CTS)] identical, it was possible to enhance the degree of their colocalization, suggesting the decisive role of this region in determining the sub-Golgi localization of enzymes. Ultimately, this study reveals the molecular codes within CTS regions as key determinants of glycosyltransferase localization, providing insights into precise control over the positioning of glycosyltransferases, and consequently, the interactions between glycosyltransferases and substrate glycoproteins as cargoes in the secretory pathway. This study advances our understanding of Golgi organization and opens avenues for programming the glycosylation of proteins for clinical applications.Key words: Golgi apparatus, glycosyltransferase, 3D super-resolution imaging, N-glycosylation.
摘要：
高尔基体,参与蛋白质加工的重要细胞器，包括糖基化，表现出复杂的子结构，即，cies-,中间,和反式水箱。这项研究通过3D超分辨率成像研究了糖基转移酶在哺乳动物细胞高尔基体中的分布。专注于参与N-聚糖修饰的人糖基转移酶，我们发现，即使假定共存于同一高尔基体区室中的酶在定位上也表现出细微的变化。通过人工制造它们的N末端区域[由细胞质组成，跨膜，和茎段（CTS）]相同，有可能提高它们的共定位程度，表明该区域在确定酶的亚高尔基体定位中的决定性作用。最终,这项研究揭示了CTS区域内的分子密码是糖基转移酶定位的关键决定因素，提供对糖基转移酶定位的精确控制的见解，因此，糖基转移酶和底物糖蛋白之间的相互作用作为分泌途径中的货物。这项研究促进了我们对高尔基体组织的理解，并为临床应用中蛋白质糖基化的编程开辟了途径。关键词:高尔基体,糖基转移酶，3D超分辨率成像，N-糖基化。
