Work

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

Year: 1997

Type: article

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.

Source: Journal of Biological Chemistry

DOI: 10.1074/jbc.272.49.30848

Authors: Bruno Antonny, Irit Huber, Sonia Paris, Marc Chabre, Dan Cassel

Institutions: Centre National de la Recherche Scientifique, Institut de Pharmacologie Moléculaire et Cellulaire, Technion – Israel Institute of Technology

Language: English

Topic: Cellular transport and secretion

Subfield: Cell Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: hybrid

Estimated APC paid: $3,430

Funders: Israel Science Foundation, Centre National de la Recherche Scientifique