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Differential Membrane Association Properties and Regulation of Class I and Class II Arfs
Author(s) -
Duijsings Daniël,
Lanke Kjerstin H. W.,
Van Dooren Sander H. J.,
Van Dommelen Michiel M. T.,
Wetzels Roy,
De Mattia Fabrizio,
Wessels Els,
Van Kuppeveld Frank J. M.
Publication year - 2009
Publication title -
traffic
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.677
H-Index - 130
eISSN - 1600-0854
pISSN - 1398-9219
DOI - 10.1111/j.1600-0854.2008.00868.x
Subject(s) - adp ribosylation factor , gtpase , biology , guanine nucleotide exchange factor , microbiology and biotechnology , gtp binding protein regulators , guanosine , biochemistry , g protein , signal transduction , endoplasmic reticulum , golgi apparatus
ADP‐ribosylation factor (Arf) proteins are small guanosine triphosphatases (GTPases) that act as major regulators of intracellular vesicular trafficking and secretory organelle pathway integrity. Like all small monomeric GTPases, Arf proteins cycle between a GDP‐bound and a GTP‐bound state, and this cycling is catalysed by guanine nucleotide exchange factors (GEFs) and GTPase‐activating proteins. While the class I Arfs, especially Arf1, have been studied extensively, little is known as yet about the function and regulation of class II Arfs, Arf4 and Arf5. In this study, we show that Arf proteins show class‐specific dynamic behaviour. Moreover, unlike class I Arfs, membrane association of class II Arfs is resistant to inhibition of large Arf GEFs by Brefeldin A. Through the construction of Arf chimeric proteins, evidence is provided that the N‐terminal amphipathic helix and a class‐specific residue in the conserved interswitch domain determine the membrane‐binding properties of class I and class II Arf proteins. Our results show that fundamental differences exist in behaviour and regulation of these small GTPases.