Binding and Functions of ADP-ribosylation Factor on Mammalian and Yeast Peroxisomes*
Binding and Functions of ADP-ribosylation Factor on Mammalian and Yeast Peroxisomes*
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ADP-核糖基化因子对哺乳动物和酵母过氧化物酶体的结合和功能*
DOI：
10.1074/jbc.m503497200
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发表时间：
2005
影响因子：
4.8
通讯作者：
W. Just
中科院分区：
文献类型：
--
作者：
D. Lay;Bianka L. Grosshans;H. Heid;K. Gorgas;W. Just
我们在体外分析了 ADP-核糖基化因子 (ARF) 蛋白家族成员与高度纯化的无高尔基体膜的大鼠肝脏过氧化物酶体制剂的结合特征，并在体内研究了这些蛋白在酵母过氧化物酶体增殖中的作用。尽管 ARF1 和 ARF6 均在过氧化物酶体上发现，但涂层异构体的招募仅取决于 ARF1-GTP。用过氧化物酶体增殖剂预处理动物以及ATP和指定为耗尽ARF和外壳体的中间库级分的胞质级分均显着影响ARF1和外壳体向过氧化物酶体的募集。在 ATP 存在下，过氧化物酶体上 ARF1 和涂层异构体的浓度降低，而中间库分数导致 ARF 浓度依赖性降低和涂层异构体增加。 Brefeldin A 是一种真菌毒素，已知可减少 ARF1 与高尔基体膜的结合，但不会影响 ARF1 与过氧化物酶体的结合。在酿酒酵母中，ScARF1 和 ScARF3（哺乳动物 ARF1 和 ARF6 的酵母直系同源物）都参与过氧化物酶体增殖的控制。 ScARF1以正向方式调节该过程，ScARF3以负向方式调节该过程。
We have analyzed in vitro the binding characteristics of members of the ADP-ribosylation factor (ARF) family of proteins to a highly purified rat liver peroxisome preparation void of Golgi membranes and studied in vivo a role these proteins play in the proliferation of yeast peroxisomes. Although both ARF1 and ARF6 were found on peroxisomes, coatomer recruitment only depended on ARF1-GTP. Recruitment of ARF1 and coatomer to peroxisomes was significantly affected both by pretreating the animals with peroxisome proliferators and by ATP and a cytosolic fraction designated the intermediate pool fraction depleted of ARF and coatomer. In the presence of ATP, the concentrations of ARF1 and coatomer on peroxisomes were reduced, whereas intermediate pool fraction led to a concentration-dependent decrease in ARF and increase in coatomer. Brefeldin A, a fungal toxin that is known to reduce ARF1 binding to Golgi membranes, did not affect ARF1 binding to peroxisomes. In Saccharomyces cerevisiae, both ScARF1 and ScARF3, the yeast orthologs of mammalian ARF1 and ARF6, were implicated in the control of peroxisome proliferation. ScARF1 regulated this process in a positive manner, and ScARF3 regulated it in a negative manner.