Molecular characterization of the GTPase-activating domain of ADP-ribosylation factor domain protein 1 (ARD1).

The Journal of Biological Chemistry
N VitaleM Vaughan

Abstract

ADP-ribosylation factors (ARFs) are approximately 20-kDa guanine nucleotide-binding proteins recognized as critical components in intracellular vesicular transport and phospholipase D activation. Both guanine nucleotide-exchange proteins and GTPase-activating proteins (GAPs) for ARFs have been cloned recently. A zinc finger motif near the amino terminus of the ARF1 GAP was required for stimulation of GTP hydrolysis. ARD1 is an ARF family member that differs from other ARFs by the presence of a 46-kDa amino-terminal extension. We had reported that the ARF domain of ARD1 binds specifically GDP and GTP and that the amino-terminal extension acts as a GAP for the ARF domain of ARD1 but not for ARF proteins. The GAP domain of ARD1, synthesized in Escherichia coli, stimulated hydrolysis of GTP bound to the ARF domain of ARD1. Using ARD1 truncations, it appears that amino acids 101-190 are critical for GAP activity, whereas residues 190-333 are involved in physical interaction between the two domains of ARD1 and are required for GTP hydrolysis. The GAP function of the amino-terminal extension of ARD1 required two arginines, an intact zinc finger motif, and a group of residues which resembles a sequence present in Rho/Rac GAPs. Interact...Continue Reading

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Citations

Aug 11, 1998·Trends in Biochemical Sciences·K ScheffzekA Wittinghofer
Jun 14, 2008·Proceedings of the National Academy of Sciences of the United States of America·Maria Zeniou-MeyerNicolas Vitale
Mar 18, 2003·Molecular and Cellular Biology·Chunzhi XiaMingyao Liu
Jul 22, 1998·Proceedings of the National Academy of Sciences of the United States of America·N VitaleM Vaughan
Oct 7, 2015·Scientific Reports·Mohamed Raafet AmmarNicolas Vitale
Aug 15, 1998·The Journal of Biological Chemistry·J Moss, M Vaughan
Nov 13, 2001·Oncogene·K JensenP S Freemont
Jan 7, 2009·The Journal of Biological Chemistry·Aurélie BégléNicolas Vitale
Jan 25, 2017·The Journal of Biological Chemistry·Nawal KassasNicolas Vitale

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