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http://purl.uniprot.org/citations/27789707http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/27789707http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/27789707http://www.w3.org/2000/01/rdf-schema#comment"The facultative intracellular pathogen Listeria monocytogenes causes listeriosis, a rare but life-threatening disease. Host cell entry begins with activation of the human receptor tyrosine kinase MET through the bacterial invasion protein InlB, which contains an internalin domain, a B-repeat, and three GW domains. The internalin domain is known to bind MET, but no interaction partner is known for the B-repeat. Adding the B-repeat to the internalin domain potentiates MET activation and is required to stimulate Madin-Darby canine kidney (MDCK) cell scatter. Therefore, it has been hypothesized that the B-repeat may bind a co-receptor on host cells. To test this hypothesis, we mutated residues that might be important for binding an interaction partner. We identified two adjacent residues in strand β2 of the β-grasp fold whose mutation abrogated induction of MDCK cell scatter. Biophysical analysis indicated that these mutations do not alter protein structure. We then tested these mutants in human HT-29 cells that, in contrast to the MDCK cells, were responsive to the internalin domain alone. These assays revealed a dominant negative effect, reducing the activity of a construct of the internalin domain and mutated B-repeat below that of the individual internalin domain. Phosphorylation assays of MET and its downstream targets AKT and ERK confirmed the dominant negative effect. Attempts to identify a host cell receptor for the B-repeat were not successful. We conclude that there is limited support for a co-receptor hypothesis and instead suggest that the B-repeat contributes to MET activation through low affinity homodimerization."xsd:string
http://purl.uniprot.org/citations/27789707http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m116.746685"xsd:string
http://purl.uniprot.org/citations/27789707http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m116.746685"xsd:string
http://purl.uniprot.org/citations/27789707http://purl.uniprot.org/core/author"Niemann H.H."xsd:string
http://purl.uniprot.org/citations/27789707http://purl.uniprot.org/core/author"Niemann H.H."xsd:string
http://purl.uniprot.org/citations/27789707http://purl.uniprot.org/core/author"Bleymueller W.M."xsd:string
http://purl.uniprot.org/citations/27789707http://purl.uniprot.org/core/author"Bleymueller W.M."xsd:string
http://purl.uniprot.org/citations/27789707http://purl.uniprot.org/core/author"Ebbes M."xsd:string
http://purl.uniprot.org/citations/27789707http://purl.uniprot.org/core/author"Ebbes M."xsd:string
http://purl.uniprot.org/citations/27789707http://purl.uniprot.org/core/author"Geerds C."xsd:string
http://purl.uniprot.org/citations/27789707http://purl.uniprot.org/core/author"Geerds C."xsd:string
http://purl.uniprot.org/citations/27789707http://purl.uniprot.org/core/author"Laemmermann N."xsd:string
http://purl.uniprot.org/citations/27789707http://purl.uniprot.org/core/author"Laemmermann N."xsd:string
http://purl.uniprot.org/citations/27789707http://purl.uniprot.org/core/author"Maynard D."xsd:string
http://purl.uniprot.org/citations/27789707http://purl.uniprot.org/core/author"Maynard D."xsd:string
http://purl.uniprot.org/citations/27789707http://purl.uniprot.org/core/date"2016"xsd:gYear
http://purl.uniprot.org/citations/27789707http://purl.uniprot.org/core/date"2016"xsd:gYear
http://purl.uniprot.org/citations/27789707http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/27789707http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/27789707http://purl.uniprot.org/core/pages"25567-25577"xsd:string
http://purl.uniprot.org/citations/27789707http://purl.uniprot.org/core/pages"25567-25577"xsd:string
http://purl.uniprot.org/citations/27789707http://purl.uniprot.org/core/title"MET-activating residues in the B-repeat of the Listeria monocytogenes invasion protein InlB."xsd:string
http://purl.uniprot.org/citations/27789707http://purl.uniprot.org/core/title"MET-activating residues in the B-repeat of the Listeria monocytogenes invasion protein InlB."xsd:string