THE ARF1 GTPASE-ACTIVATING PROTEIN - ZINC-FINGER MOTIF AND GOLGI-COMPLEX LOCALIZATION
THE ARF1 GTPASE-ACTIVATING PROTEIN - ZINC-FINGER MOTIF AND GOLGI-COMPLEX LOCALIZATION
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DOI：
10.1126/science.270.5244.1999
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发表时间：
1995-12-22
期刊：
影响因子：
56.9
通讯作者：
CASSEL, D
中科院分区：
文献类型：
--
作者：
CUKIERMAN, E;HUBER, I;CASSEL, D
三磷酸鸟苷（GTP）被小的三磷酸鸟苷酶（GT3）二磷酸腺苷核糖基化因子-1（ARF 1）水解依赖于GTP酶激活蛋白（GAP）。从大鼠肝脏中克隆了编码ARF 1 GAP的互补DNA，并预测在氨基末端附近具有锌指基序的蛋白质。差距功能需要一个完整的锌指和额外的氨基末端残基。ARF 1 GAP定位于高尔基复合体，当细胞用布雷菲德菌素A（一种阻止ARF 1依赖性外壳蛋白与高尔基体结合的药物）处理时，重新分布到胞质模式中。因此，差距很可能通过依赖于ARF 1的机制被募集到高尔基体。
Hydrolysis of guanosine triphosphate (GTP) by the small guanosine triphosphatase (GTPase) adenosine diphosphate ribosylation factor-1 (ARF1) depends on a GTPase-activating protein (GAP). A complementary DNA encoding the ARF1 GAP was cloned from rat liver and predicts a protein with a zinc finger motif near the amino terminus. The GAP function required an intact zinc finger and additional amino-terminal residues. The ARF1 GAP was localized to the Golgi complex and was redistributed into a cytosolic pattern when cells were treated with brefeldin A, a drug that prevents ARF1-dependent association of coat proteins with the Golgi. Thus, the GAP is likely to be recruited to the Golgi by an ARF1-dependent mechanism.