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ARF-Directed Guanine-Nucleotide-Exchange (GEP) Proteins

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GTPase Protocols

Part of the book series: Methods in Molecular Biology™ ((MIMB,volume 189))

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Abstract

TheADP-ribosylation factor proteins (ARFs) are ~20-kDa guanine-nucleotidebinding proteins found in all eukaryotic cells, which are a critical part of the minimum machinery required for vesicle formation at the Golgi and other membranes (1–3). The six mammalian ARFs have been grouped into three classes (4) based on molecular size, amino-acid sequence, and gene structure: class I (ARF1-3), class II (ARF4, 5), and class III (ARF6). Proteins closely related to ARFs include ARF-like proteins (ARLs), ARF-related protein (ARP), and ARF-domain protein 1 (ARD1) (5). ARFs function as activators of choleratoxin ADP-ribosyltransferase and phospholipase D (PLD) (6,7), and have been recently implicated in the activation of phosphatidylinositol 4-phosphate 5-kinase (8). ARF, like other regulatory GTPases, is active when GTP is bound. The inactivation of ARF-GTP requires its interaction with a GTPase-activating protein (GAP), which accelerates GTP hydrolysis. Activation of the inactive GDP-bound ARF requires the action of a guanine nucleotide-exchange protein or GEP, which accelerates the release of bound nucleotide via stabilization of the guanine nucleotide-free protein (9).

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Authors and Affiliations

  1. Pulmonary-Critical Care Medicine Branch, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD

    Gustavo Pacheco-Rodriguez, Joel Moss & Martha Vaughan

Authors
  1. Gustavo Pacheco-Rodriguez
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  2. Joel Moss
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  3. Martha Vaughan
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Editors and Affiliations

  1. Glaxo-IMCB Group, Institute of Molecular and Cell Biology, Singapore

    Ed Manser  & Thomas Leung  & 

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© 2002 Humana Press Inc.

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Pacheco-Rodriguez, G., Moss, J., Vaughan, M. (2002). ARF-Directed Guanine-Nucleotide-Exchange (GEP) Proteins. In: Manser, E., Leung, T. (eds) GTPase Protocols. Methods in Molecular Biology™, vol 189. Springer, Totowa, NJ. https://doi.org/10.1385/1-59259-281-3:181

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  • DOI: https://doi.org/10.1385/1-59259-281-3:181

  • Publisher Name: Springer, Totowa, NJ

  • Print ISBN: 978-0-89603-934-6

  • Online ISBN: 978-1-59259-281-4

  • eBook Packages: Springer Protocols

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