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The ARF1 GTPase-Activating Protein: Zinc Finger Motif and Golgi Complex Localization
Abstract
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.
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Helms, J. B., & Rothman, J. E. (1992) · Nature · doi:10.1038/360352a0 · Cited by 746
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Metadata
- Authors
- Cukierman, E., Huber, I., Rotman, M., & Cassel, D.
- Venue
- Science
- Published
- 1995-12-22
- Volume
- 270
- Issue
- 5244
- Pages
- 1999-2002
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1976579206
- Cited by
- 340
- References
- 1
- FWCI
- 5.90
- Type
- journal article
- Language
- en
- Open access
- closed
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- Cukierman, E., Huber, I., Rotman, M., & Cassel, D. (1995). The ARF1 GTPase-Activating Protein: Zinc Finger Motif and Golgi Complex Localization. Science. https://doi.org/10.1126/science.270.5244.1999
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