GGA proteins associate with Golgi membranes through interaction between their GGAH domains and ADP-ribosylation factors.
GGA proteins associate with Golgi membranes through interaction between their GGAH domains and ADP-ribosylation factors.
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GGA 蛋白通过其 GGAH 结构域和 ADP 核糖基化因子之间的相互作用与高尔基体膜结合。
DOI：
10.1042/bj20020428
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发表时间：
2002
期刊：
影响因子：
--
通讯作者：
K. Nakayama
中科院分区：
文献类型：
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作者：
H. Takatsu;K. Yoshino;Kyoko Toda;K. Nakayama
ADP-核糖基化因子 (ARF) 是一个小 GTP 酶家族，参与膜运输事件的各个方面。其中包括ARF1-ARF6，根据一级结构的相似性分为三类：I类，ARF1-ARF3； II 类，ARF4 和 ARF5；和 III 类，ARF6。先前的研究发现了一个新的潜在ARF效应子家族，称为GGA1-GGA3，它们与GTP结合的ARF1和ARF3特异性相互作用，并定位于跨高尔基体网络（TGN）或其相关区室（GGA是高尔基体定位、γ-适应素耳朵同源结构域、ARF结合蛋白的缩写）。在本研究中，我们表明，属于三类 ARF1、ARF5 和 ARF6 的 ARF 蛋白可以在体外和体内酵母双杂交测定中与所有 GGA 蛋白相互作用。 GGA 蛋白的分割和 ARF 结合缺陷的 GGA 突变体的分离表明，GGA 同源结构域内的有限区域（在 GGA 家族中保守）对于 ARF 结合至关重要。 ARF1 和 ARF5 的 GTP 酶限制突变体在细胞中的表达可阻断布雷菲德菌素 A 诱导的 GGA 蛋白从膜上的解离。然而，这两种 ARF 突变体都不会招募 ARF 结合缺陷的 GGA 突变体。根据这些观察结果，我们得出结论，至少处于 GTP 结合状态的 ARF1（I 类）和 ARF5（II 类）会导致 GGA 蛋白募集到 TGN 膜上。相反，根据类似的实验，ARF6（III类）可能参与将GGA蛋白募集到其他区室，可能是早期内体。
ADP-ribosylation factors (ARFs) are a family of small GTPases that are involved in various aspects of membrane trafficking events. These include ARF1-ARF6, which are divided into three classes on the basis of similarity in the primary structure: Class I, ARF1-ARF3; Class II, ARF4 and ARF5; and Class III, ARF6. Previous studies identified a novel family of potential ARF effectors, termed GGA1-GGA3, which interact specifically with GTP-bound ARF1 and ARF3 and are localized to the trans-Golgi network (TGN) or its related compartment(s) (GGA is an abbreviation for Golgi-localizing, gamma-adaptin ear homology domain, ARF-binding protein). In the present study we have shown that ARF proteins belonging to the three classes, ARF1, ARF5 and ARF6, can interact with all GGA proteins in a yeast two-hybrid assay, in vitro and in vivo. Segmentation of GGA proteins and isolation of GGA mutants defective in ARF binding have revealed that a limited region within the GGA homology domain, which is conserved in the GGA family, is essential for ARF binding. Expression in cells of GTPase-restricted mutants of ARF1 and ARF5 blocks dissociation of GGA proteins from membranes induced by brefeldin A. However, neither of the ARF mutants recruits GGA mutants defective in ARF binding. On the basis of these observations, we conclude that at least ARF1 (Class I) and ARF5 (Class II) in their GTP-bound state cause recruitment of GGA proteins on to TGN membranes. In contrast, on the basis of similar experiments, ARF6 (Class III) may be involved in recruitment of GGA proteins to other compartments, possibly early endosomes.
DOI：
10.1101/gr.2.1.28
发表时间：
1992-08-01
期刊：
PCR methods and applications
影响因子：
--
作者：
Cadwell, R C;Joyce, G F
通讯作者：
Joyce, G F