Activation of toxin ADP-ribosyltransferases by the family of ADP-ribosylation factors

Advances in Experimental Medicine and Biology
M Vaughan, J Moss

Abstract

ADP-ribosylation factors or ARFs are 20-kDa guanine nucleotide-binding proteins, initially identified as stimulators of cholera toxin-catalyzed ADP-ribosylation of Gs alpha. We now know that ARFs play a critical role in many vesicular trafficking events and ARF activation of a membrane-associated phospholipase D (PLD) has been recognized. ARF is active and associates with membranes when GTP is bound. The active state is terminated by hydrolysis of bound GTP, producing inactive ARF-GDP. The nucleotide effect on ARF association with membranes is related to alteration in orientation of the N-terminal myristoyl moiety that is important for ARF function. Cycling of ARF between active and inactive states involves guanine nucleotide-exchange proteins (GEPs) that accelerate replacement of bound GDP with GTP and GTPase-activating proteins (GAPS) that are responsible for ARF inactivation. Six mammalian ARFs have been identified by cDNA cloning. Class I ARFs 1 and 3 have been studied most extensively. Their activation (GTP binding) is catalyzed by a GEP now purified from spleen cytosol. In crude preparations, GEP was inhibited by brefeldin A (BFA), which in cells causes apparent disintegration of Golgi. Demonstration that the approximatel...Continue Reading

Citations

Feb 16, 2002·The Journal of Biological Chemistry·Francesca BartoliniNicholas J Cowan
Sep 9, 2006·Microbiology and Molecular Biology Reviews : MMBR·Paul O HassaMichael O Hottiger
Feb 21, 2008·PloS One·Annelise SahinGilles Merlin
Apr 15, 2014·Cellular and Molecular Life Sciences : CMLS·John WrightElizabeth Sztul
Apr 12, 2000·Critical Reviews in Oral Biology and Medicine : an Official Publication of the American Association of Oral Biologists·E L Watson

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