Bette-Bobillo P, Giro P, Sainte-Marie J, Vidal M
UMR 5539 CNRS, Université Montpellier II, France.
Biochem Biophys Res Commun. 1998 Mar 17;244(2):336-41. doi: 10.1006/bbrc.1998.8263.
ADP-ribosylation of rab proteins by exoenzyme S (Exo S) of P. aeruginosa was studied using reticulocytes. 14-3-3 protein, the eukaryotic cofactor that is obligatory for Exo S activity, was found in association with reticulocyte endocytic vesicles and exosomes, vesicles previously shown to be enriched with rab4. Incubation of purified endocytic vesicles with Exo S triggered rab4 ADP-ribosylation. Transferrin recycling in SLO-permeabilized reticulocytes was highly impaired when Exo S was added to the cells, suggesting that ADP-ribosylation affected rab4 function. Moreover, in vitro ADP-ribosylation of different rab proteins was studied using the cofactor activity extracted from reticulocytes.
