THE ARF1 GTPASE-ACTIVATING PROTEIN - ZINC-FINGER MOTIF AND GOLGI-COMPLEX LOCALIZATION

被引：272

作者：

CUKIERMAN, E ^{[1
]}

HUBER, I ^{[1
]}

ROTMAN, M ^{[1
]}

CASSEL, D ^{[1
]}

机构：

[1] TECHNION ISRAEL INST TECHNOL, DEPT BIOL, IL-32000 HAIFA, ISRAEL

来源：

SCIENCE | 1995年 / 270卷 / 5244期

关键词：

D O I：

10.1126/science.270.5244.1999

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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.

引用

页码：1999 / 2002

页数：4

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