| http://purl.uniprot.org/citations/16889625 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16889625 | http://www.w3.org/2000/01/rdf-schema#comment | "Pseudomonas aeruginosa causes life-threatening infections in compromised and cystic fibrosis patients. Pathogenesis stems from a number of virulence factors, including four type III translocated cytotoxins: ExoS, ExoT, ExoY and ExoU. ExoS is a bifunctional toxin: the N terminus (amino acids 96-219) encodes a Rho GTPase Activating Protein (GAP) domain. The C terminus (amino acids 234-453) encodes a 14-3-3-dependent ADP-ribosyltransferase domain which transfers ADP-ribose from NAD onto substrates such as the Ras GTPases and vimentin. Ezrin/radixin/moesin (ERM) proteins have recently been identified as high-affinity substrates for ADP-ribosylation by ExoS. Expression of ExoS in HeLa cells led to a loss of phosphorylation of ERM proteins that was dependent upon the expression of ADP-ribosyltransferase activity. MALDI-MS and site-directed mutagenesis studies determined that ExoS ADP-ribosylated moesin at three C-terminal arginines (Arg553, Arg560 and Arg563), which cluster Thr558, the site of phosphorylation by protein kinase C and Rho kinase. ADP-ribosylated-moesin was a poor target for phosphorylation by protein kinase C and Rho kinase, which showed that ADP-ribosylation directly inhibited ERM phosphorylation. Expression of dominant active-moesin inhibited cell rounding elicited by ExoS, indicating that moesin is a physiological target in cultured cells. This is the first demonstration that a bacterial toxin inhibits the phosphorylation of a mammalian protein through ADP-ribosylation. These data explain how the expression of the ADP-ribosylation of ExoS modifies the actin cytoskeleton and indicate that ExoS possesses redundant enzymatic activities to depolymerize the actin cytoskeleton."xsd:string |
| http://purl.uniprot.org/citations/16889625 | http://purl.org/dc/terms/identifier | "doi:10.1111/j.1462-5822.2006.00770.x"xsd:string |
| http://purl.uniprot.org/citations/16889625 | http://purl.uniprot.org/core/author | "Barbieri J.T."xsd:string |
| http://purl.uniprot.org/citations/16889625 | http://purl.uniprot.org/core/author | "Deng Q."xsd:string |
| http://purl.uniprot.org/citations/16889625 | http://purl.uniprot.org/core/author | "Maresso A.W."xsd:string |
| http://purl.uniprot.org/citations/16889625 | http://purl.uniprot.org/core/author | "Wakim B.T."xsd:string |
| http://purl.uniprot.org/citations/16889625 | http://purl.uniprot.org/core/author | "Pereckas M.S."xsd:string |
| http://purl.uniprot.org/citations/16889625 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
| http://purl.uniprot.org/citations/16889625 | http://purl.uniprot.org/core/name | "Cell Microbiol"xsd:string |
| http://purl.uniprot.org/citations/16889625 | http://purl.uniprot.org/core/pages | "97-105"xsd:string |
| http://purl.uniprot.org/citations/16889625 | http://purl.uniprot.org/core/title | "Pseudomonas aeruginosa ExoS ADP-ribosyltransferase inhibits ERM phosphorylation."xsd:string |
| http://purl.uniprot.org/citations/16889625 | http://purl.uniprot.org/core/volume | "9"xsd:string |
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