The ARF1 GTPase-Activating protein: Zinc finger motif and golgi complex localization

Edna Cukierman, Irit Huber, Miriam Rotman, Dan Cassel

Research output: Contribution to journalShort surveypeer-review

276 Scopus citations

Abstract

Hydrolysis of guanosine triphosphate (GTP) by the small guanosine triphosphatase (GTPase) adenosine diphosphate ribosylation factor-1 (ARF1) depends on a GTPaseactivating 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.

Original languageEnglish
Pages (from-to)1999-2002
Number of pages4
JournalScience
Volume270
Issue number5244
DOIs
StatePublished - Dec 22 1995

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