Signal-mediated dynamic retention of glycosyltransferases in the Golgi
Signal-mediated dynamic retention of glycosyltransferases in the Golgi
复制标题
DOI：
10.1126/science.1159411
复制
发表时间：
2008-07-18
期刊：
影响因子：
56.9
通讯作者：
Banfield, David K.
中科院分区：
文献类型：
--
作者：
Tu, Linna;Tai, William C. S.;Banfield, David K.
高尔基体驻留糖基转移酶是以亚区室特异性方式顺序修饰糖蛋白的酶家族。这些II型整合膜蛋白的特征在于短的胞质暴露的氨基末端尾和管腔酶结构域。胞质尾在糖基转移酶的定位中起作用，并且外壳蛋白复合物I（COPI）囊泡介导的逆行运输也参与它们的高尔基体定位。然而，这些酶的尾部缺乏已知的COPI结合基序。在这里，我们发现，Vps74p绑定到一个五聚体基序存在于大多数的酵母高尔基体定位的糖基转移酶的细胞质尾部，以及COPI。我们建议，Vps74p保持动态的高尔基体糖基转移酶的稳态定位，通过促进其纳入COPI包被囊泡。
Golgi-resident glycosyltransferases are a family of enzymes that sequentially modify glycoproteins in a subcompartment-specific manner. These type II integral membrane proteins are characterized by a short cytoplasmically exposed amino-terminal tail and a luminal enzymatic domain. The cytoplasmic tails play a role in the localization of glycosyltransferases, and coat protein complex I (COPI) vesicle-mediated retrograde transport is also involved in their Golgi localization. However, the tails of these enzymes lack known COPI-binding motifs. Here, we found that Vps74p bound to a pentameric motif present in the cytoplasmic tails of the majority of yeast Golgi-localized glycosyltransferases, as well as to COPI. We propose that Vps74p maintains the steady-state localization of Golgi glycosyltransferases dynamically, by promoting their incorporation into COPI-coated vesicles.