Yeast Dop1 is required for glycosyltransferase retrieval from the trans-Golgi network
Yeast Dop1 is required for glycosyltransferase retrieval from the trans-Golgi network
复制标题
从跨高尔基体网络中检索糖基转移酶需要酵母 Dop1
DOI：
10.1016/j.bbagen.2019.04.009
复制
发表时间：
2019
影响因子：
3
通讯作者：
Fujita Morihisa
中科院分区：
文献类型：
--
作者：
Zhao Shen-Bao;Suda Yasuyuki;Nakanishi Hideki;Wang Ning;Yoko-o Takehiko;Gao Xiao-Dong;Fujita Morihisa
背景糖基转移酶是一种II型膜蛋白，负责蛋白质和脂质的聚糖修饰，并定位于高尔基体的不同池中。在脑池成熟过程中，逆行贩运有助于保持这些酶的稳定状态本地化的子隔室的Golgi.MethodsTo了解糖基转移酶是如何回收的后期高尔基复合体，我们寻找的基因是必不可少的芽殖酵母细胞生长和编码蛋白质定位在内体和高尔基体。结果Dop 1主要定位于高尔基体网络（trans-Golgi network，TGN）的年轻区室，并在TGN内循环。与此相反，Neo 1，一种与Dop 1相互作用的P4-ATP酶，定位于TGN。DOP 1表达的消除导致FM 4 -64内吞途径的缺陷。Dop 1和Neo 1是高尔基体上转化酶（一种分泌蛋白）正确糖基化所必需的。在DOP 1关闭细胞，Och 1，甘露糖基转移酶，通常位于卵泡膜-高尔基体，错误定位到TGN。此外，N-和O-糖基化所需的多个糖基转移酶的功能受损inDOP 1-shutdown cells.ConclusionsOur结果表明，Dop 1参与囊泡运输在TGN，是关键的检索糖基转移酶从TGN到高尔基体在yeast.General significance高尔基体驻留糖基转移酶回收从TGN到高尔基体依赖于Dop 1和P4-ATP酶Neo 1。
BackgroundGlycosyltransferases are type II membrane proteins that are responsible for glycan modification of proteins and lipids, and localize to distinct cisternae in the Golgi apparatus. During cisternal maturation, retrograde trafficking helps maintain the steady-state localization of these enzymes in the sub-compartments of the Golgi.MethodsTo understand how glycosyltransferases are recycled in the late Golgi complex, we searched for genes that are essential for budding yeast cell growth and that encode proteins localized in endosomes and in the Golgi. We specifically analyzed the roles of Dop1 and its binding partner Neo1 in retaining Golgi-resident glycosyltransferases, in the late Golgi complex.ResultsDop1 primarily localized to younger compartments of thetrans-Golgi network (TGN) and seemed to cycle within the TGN. In contrast, Neo1, a P4-ATPase that interacts with Dop1, localized to the TGN. Abolition ofDOP1expression led to defects in the FM4-64 endocytic pathway. Dop1 and Neo1 were required for correct glycosylation of invertase, a secretory protein, at the Golgi. InDOP1-shutdown cells, Och1, a mannosyltransferase that is typically located in thecis-Golgi, mislocalized to the TGN. In addition, the function of multiple glycosyltransferases required for N- and O-glycosylation were impaired inDOP1-shutdown cells.ConclusionsOur results indicate that Dop1 is involved in vesicular transport at the TGN, and is critical for retrieving glycosyltransferases from the TGN to the Golgi in yeast.General significanceGolgi-resident glycosyltransferases recycling from the TGN to the Golgi is dependent on Dop1 and the P4-ATPase Neo1.