BREFELDIN-A INHIBITS GOLGI MEMBRANE-CATALYZED EXCHANGE OF GUANINE-NUCLEOTIDE ONTO ARF PROTEIN
BREFELDIN-A INHIBITS GOLGI MEMBRANE-CATALYZED EXCHANGE OF GUANINE-NUCLEOTIDE ONTO ARF PROTEIN
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DOI：
10.1038/360350a0
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发表时间：
1992-11-26
期刊：
影响因子：
64.8
通讯作者：
KLAUSNER, RD
中科院分区：
文献类型：
--
作者：
DONALDSON, JG;FINAZZI, D;KLAUSNER, RD
真菌代谢物布雷菲德菌素A是研究真核细胞膜运输的有力工具1。布雷菲德菌素A对交通的影响部分地通过其阻止细胞溶质外壳蛋白结合到膜上的能力来解释2 -5。非网格蛋白被衣体复合物6，7在GTP控制的周期中可逆地结合高尔基体膜8 -10。低分子量GTP结合蛋白ADP-核糖基化因子（ARF），也可逆地与高尔基体膜11，12相关联，是外套体结合所需的13，并可能占外套体-膜相互作用的鸟嘌呤核苷酸的控制。布雷菲德菌素A通过抑制ARF与高尔基体膜的GTP依赖性相互作用13来阻止被膜分子在膜上的组装，但这种相互作用的性质尚未确定。在这里，我们证明了高尔基体膜可以特异性地催化GTP交换到ARF上，而布雷菲德菌素A阻止了这一功能。
THE fungal metabolite brefeldin A is a powerful tool for investigating membrane traffic in eukaryotic cells1. The effects of brefeldin A on traffic are partly explained by its ability to prevent binding of cytosolic coat proteins onto membranes2-5. The non-clathrin coatomer complex6,7 binds reversibly to Golgi membranes in a GTP-controlled cycle8-10. The low-molecular-mass GTP-binding protein ADP-ribosylation factor (ARF), which also associates reversibly with Golgi membranes11,12, is required for coatomer binding13 and probably accounts for the control by guanine nucleotide of the coatomer-membrane interaction. Brefeldin A prevents the assembly of coatomer onto the membrane by inhibiting the GTP-dependent interaction of ARF with the Golgi membrane13, but the nature of this interaction has not been established. Here we demonstrate that Golgi membranes can specifically catalyse the exchange of GTP onto ARF and that brefeldin A prevents this function.