Modulatory role of GTP-binding proteins in the endogenous ADP-ribosylation of cytosolic proteins

Advances in Experimental Medicine and Biology
M Di GirolamoD Corda

Abstract

The endogenous ADP-ribosylation of cytosolic proteins and the pattern of NAD degradation were analyzed in subcellular fractions of rat liver in order to investigate the modulation of these reactions by GTP-binding (G) proteins. We could show that intracellular membranes from rat liver have a guanine nucleotide- and divalent cation-dependent pyrophosphatase activity able to rapidly degrade NAD to AMP. This enzymatic activity was investigated by two different approaches: the degradation of [32P]-NAD in the presence of intracellular membranes and the mono-ADP-ribosylation of cytosolic proteins. Divalent cations, preferentially Zn2+ and Mn2+, were required for the pyrophosphatase activity, since in the presence of the Zn2+ chelator TPEN (N,N,N',N'-tetrakis(2-pyridyl-methyl)ethylenediamine) or EDTA, the NAD degradation was inhibited by about 50%. Accordingly, in the presence of TPEN the endogenous ADP-ribosylation of cytosolic proteins was enhanced, whereas Zn2+ caused a significant inhibition of this reaction. GDP beta S was able to strongly activate the mono-ADP-ribosylation of cytosolic proteins. This effect was abolished by GTP gamma S, suggesting that a G protein, or rather one of the subunits of a heterotrimeric G protein, is ...Continue Reading

Citations

Feb 22, 2012·The Journal of Physiology·Leonie DurninVioleta N Mutafova-Yambolieva
Oct 5, 2007·Proceedings of the National Academy of Sciences of the United States of America·Violeta N Mutafova-YambolievaKenton M Sanders
Sep 29, 2005·American Journal of Physiology. Renal Physiology·Leanne T BreenVioleta N Mutafova-Yambolieva

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