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http://purl.uniprot.org/citations/16176924http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16176924http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16176924http://www.w3.org/2000/01/rdf-schema#comment"Salmonella translocate bacterial effectors into host cells to confer bacterial entry and survival. It is not known how the host cells cope with the influx of these effectors. We report here that the Salmonella effector, SopA, interacts with host HsRMA1, a ubiquitin E3 ligase with a previously unknown function. SopA is ubiquitinated and degraded by the HsRMA1-mediated ubiquitination pathway. A sopA mutant escapes out of the Salmonella-containing vacuoles less frequently to the cytosol than wild type Salmonella in HeLa cells in a HsRMA1-dependent manner. Our data suggest that efficient bacterial escape into the cytosol of epithelial cells requires HsRMA1-mediated SopA ubiquitination and contributes to Salmonella-induced enteropathogenicity."xsd:string
http://purl.uniprot.org/citations/16176924http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m506309200"xsd:string
http://purl.uniprot.org/citations/16176924http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m506309200"xsd:string
http://purl.uniprot.org/citations/16176924http://purl.uniprot.org/core/author"Zhang Y."xsd:string
http://purl.uniprot.org/citations/16176924http://purl.uniprot.org/core/author"Zhang Y."xsd:string
http://purl.uniprot.org/citations/16176924http://purl.uniprot.org/core/author"Zhou D."xsd:string
http://purl.uniprot.org/citations/16176924http://purl.uniprot.org/core/author"Zhou D."xsd:string
http://purl.uniprot.org/citations/16176924http://purl.uniprot.org/core/author"Dai S."xsd:string
http://purl.uniprot.org/citations/16176924http://purl.uniprot.org/core/author"Dai S."xsd:string
http://purl.uniprot.org/citations/16176924http://purl.uniprot.org/core/author"Sherman D.M."xsd:string
http://purl.uniprot.org/citations/16176924http://purl.uniprot.org/core/author"Sherman D.M."xsd:string
http://purl.uniprot.org/citations/16176924http://purl.uniprot.org/core/author"Higashide W."xsd:string
http://purl.uniprot.org/citations/16176924http://purl.uniprot.org/core/author"Higashide W."xsd:string
http://purl.uniprot.org/citations/16176924http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/16176924http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/16176924http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/16176924http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/16176924http://purl.uniprot.org/core/pages"38682-38688"xsd:string
http://purl.uniprot.org/citations/16176924http://purl.uniprot.org/core/pages"38682-38688"xsd:string
http://purl.uniprot.org/citations/16176924http://purl.uniprot.org/core/title"Recognition and ubiquitination of Salmonella type III effector SopA by a ubiquitin E3 ligase, HsRMA1."xsd:string
http://purl.uniprot.org/citations/16176924http://purl.uniprot.org/core/title"Recognition and ubiquitination of Salmonella type III effector SopA by a ubiquitin E3 ligase, HsRMA1."xsd:string
http://purl.uniprot.org/citations/16176924http://purl.uniprot.org/core/volume"280"xsd:string
http://purl.uniprot.org/citations/16176924http://purl.uniprot.org/core/volume"280"xsd:string