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Science 22 December 1995:
Vol. 270. no. 5244, pp. 1999 - 2002
DOI: 10.1126/science.270.5244.1999
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Reports

The ARF1 GTPase-Activating Protein: Zinc Finger Motif and Golgi Complex Localization

Edna Cukierman,  Irit Huber,  Miriam Rotman,  Dan Cassel (1)

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.


Department of Biology, Technion-Israel Institute of Technology, Haifa 32000, Israel.
(1) To whom correspondence should be addressed. E-mail: bir06dc{at}technion.technion.ac.il


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Sorting of Golgi resident proteins into different subpopulations of COPI vesicles: a role for ArfGAP1.
J. Lanoix, J. Ouwendijk, A. Stark, E. Szafer, D. Cassel, K. Dejgaard, M. Weiss, and T. Nilsson (2001)
J. Cell Biol. 155, 1199-1212
   Abstract »    Full Text »    PDF »
The Gcs1 and Age2 ArfGAP proteins provide overlapping essential function for transport from the yeast trans-Golgi network.
P. P. Poon, S. F. Nothwehr, R. A. Singer, and G. C. Johnston (2001)
J. Cell Biol. 155, 1239-1250
   Abstract »    Full Text »    PDF »


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