GTP-bound forms of rab6 induce the redistribution of Golgi proteins into the endoplasmic reticulum
GTP-bound forms of rab6 induce the redistribution of Golgi proteins into the endoplasmic reticulum
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DOI：
10.1073/pnas.94.5.1828
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发表时间：
1997-03-04
影响因子：
11.1
通讯作者：
Goud, B
中科院分区：
文献类型：
--
作者：
Martinez, O;Antony, C;Goud, B
rab6 是一种普遍存在的 ras 样 GTP 酶，参与高尔基体内转运，我们在形态学和生化水平上研究了高尔基体驻留蛋白在过表达野生型 rab6 以及 rab6 的 GTP 和 GDP 结合突变体（分别为 rab6 Q72L 和 rab6 T27N）的 HeLa 细胞中的行为，我们表明野生型 rab6 和 rab6 Q72L 过表达会诱导 redistribution of the trans-Golgi protein beta-1,4-galactosyltransferase into the endoplasmic reticulum (ER) and allows the addition of sialylated O-glycans on an ER-retained protein, the major histocompatibility complex class II-associated invariant chain. Remarkably, rab6 Q72L effects, which require the integrity of microtubules, were almost indistinguishable from those induced by brefeldin A, a fungic metabolite that causes a mixing of Golgi and ER membranes. In contrast, overexpression of rab6 T27N does not cause the redistribution of Golgi proteins, but inhibits basal O-glycosylation of the major histocompatibility complex class II-associated invariant chain.
rab6 is a ubiquitous ras-like GTPase involved in intra-Golgi transport, We have studied at both morphological and biochemical levels the behavior of Golgi resident proteins in HeLa cells overexpressing wild-type rab6 and GTP- and GDP-bound mutants of rab6 (rab6 Q72L and rab6 T27N, respectively), We show that wild-type rab6 and rab6 Q72L overexpression induces the redistribution of the trans-Golgi protein beta-1,4-galactosyltransferase into the endoplasmic reticulum (ER) and allows the addition of sialylated O-glycans on an ER-retained protein, the major histocompatibility complex class II-associated invariant chain. Remarkably, rab6 Q72L effects, which require the integrity of microtubules, were almost indistinguishable from those induced by brefeldin A, a fungic metabolite that causes a mixing of Golgi and ER membranes. In contrast, overexpression of rab6 T27N does not cause the redistribution of Golgi proteins, but inhibits basal O-glycosylation of the major histocompatibility complex class II-associated invariant chain.