Exoenzyme S from P. aeruginosa ADP ribosylates rab4 and inhibits transferrin recycling in SLO-permeabilized reticulocytes
| Autor: | Pascale Bette-Bobillo, Josette Sainte-Marie, Michel Vidal, Pierre Giro |
|---|---|
| Rok vydání: | 1998 |
| Předmět: |
Cell Membrane Permeability
Reticulocytes Tyrosine 3-Monooxygenase Bacterial Toxins Molecular Sequence Data Biophysics Coenzymes In Vitro Techniques Biochemistry Cofactor Reticulocyte Bacterial Proteins GTP-Binding Proteins Consensus Sequence medicine Animals Amino Acid Sequence Molecular Biology chemistry.chemical_classification ADP Ribose Transferases Adenosine Diphosphate Ribose biology rab4 GTP-Binding Proteins Vesicle fungi Transferrin Proteins Cell Biology Microvesicles In vitro Cell biology Rats medicine.anatomical_structure Endocytic vesicle chemistry 14-3-3 Proteins Pseudomonas aeruginosa Streptolysins biology.protein Rab Poly(ADP-ribose) Polymerases |
| Zdroj: | Biochemical and biophysical research communications. 244(2) |
| ISSN: | 0006-291X |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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