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Activation of ADP-ribosylation Factor 1 GTPase-Activating Protein by Phosphatidylcholine-derived Diacylglycerols

Open access
Antonny, Bruno, Huber, Irit, Paris, Sonia, Chabre, Marc, Cassel, Dan·1997·Journal of Biological Chemistry

Abstract

Disassembly of the coatomer from Golgi vesicles requires that the small GTP-binding protein ADP-ribosylation factor 1 (ARF1) hydrolyzes its bound GTP by the action of a GTPase-activating protein. In vitro, the binding of the ARF1 GTPase-activating protein to lipid vesicles and its activity on membrane-bound ARF1GTP are increased by diacylglycerols with monounsaturated acyl chains, such as those arising in vivo as secondary products from the hydrolysis of phosphatidylcholine by ARF-activated phospholipase D. Thus, the phospholipase D pathway may provide a feedback mechanism that promotes GTP hydrolysis on ARF1 and the consequent uncoating of vesicles.

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Metadata

Authors
Antonny, B., Huber, I., Paris, S., Chabre, M., & Cassel, D.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1997-12
Volume
272
Issue
49
Pages
30848-30851
ISSN
0021-9258 (ISSN-L)
OpenAlex
W2061669611
Cited by
166
References
0
FWCI
3.14
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Activation of ADP-ribosylation Factor 1 GTPase-Activating Protein by Phosphatidylcholine-derived Diacylglycerols. https://app.cochat.ai/papers/10.1074/jbc.272.49.30848
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Antonny, B., Huber, I., Paris, S., Chabre, M., & Cassel, D. (1997). Activation of ADP-ribosylation Factor 1 GTPase-Activating Protein by Phosphatidylcholine-derived Diacylglycerols. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.272.49.30848

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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