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http://purl.uniprot.org/citations/35222471http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/35222471http://www.w3.org/2000/01/rdf-schema#comment"Tyrosine-specific protein tyrosine phosphatases (Tyr-specific PTPases) are key signaling enzymes catalyzing the removal of the phosphate group from phosphorylated tyrosine residues on target proteins. This post-translational modification notably allows the regulation of mitogen-activated protein kinase (MAPK) cascades during defense reactions. Arabidopsis thaliana protein tyrosine phosphatase 1 (AtPTP1), the only Tyr-specific PTPase present in this plant, acts as a repressor of H2O2 production and regulates the activity of MPK3/MPK6 MAPKs by direct dephosphorylation. Here, we report that recombinant histidine (His)-AtPTP1 protein activity is directly inhibited by H2O2 and nitric oxide (NO) exogenous treatments. The effects of NO are exerted by S-nitrosation, i.e., the formation of a covalent bond between NO and a reduced cysteine residue. This post-translational modification targets the catalytic cysteine C265 and could protect the AtPTP1 protein from its irreversible oxidation by H2O2. This mechanism of protection could be a conserved mechanism in plant PTPases."xsd:string
http://purl.uniprot.org/citations/35222471http://purl.org/dc/terms/identifier"doi:10.3389/fpls.2022.807249"xsd:string
http://purl.uniprot.org/citations/35222471http://purl.uniprot.org/core/author"Rossi J."xsd:string
http://purl.uniprot.org/citations/35222471http://purl.uniprot.org/core/author"Pichereaux C."xsd:string
http://purl.uniprot.org/citations/35222471http://purl.uniprot.org/core/author"Astier J."xsd:string
http://purl.uniprot.org/citations/35222471http://purl.uniprot.org/core/author"Rosnoblet C."xsd:string
http://purl.uniprot.org/citations/35222471http://purl.uniprot.org/core/author"Wendehenne D."xsd:string
http://purl.uniprot.org/citations/35222471http://purl.uniprot.org/core/author"Nicolas-Frances V."xsd:string
http://purl.uniprot.org/citations/35222471http://purl.uniprot.org/core/author"Besson-Bard A."xsd:string
http://purl.uniprot.org/citations/35222471http://purl.uniprot.org/core/author"Klinguer A."xsd:string
http://purl.uniprot.org/citations/35222471http://purl.uniprot.org/core/author"Hichami S."xsd:string
http://purl.uniprot.org/citations/35222471http://purl.uniprot.org/core/date"2022"xsd:gYear
http://purl.uniprot.org/citations/35222471http://purl.uniprot.org/core/name"Front Plant Sci"xsd:string
http://purl.uniprot.org/citations/35222471http://purl.uniprot.org/core/pages"807249"xsd:string
http://purl.uniprot.org/citations/35222471http://purl.uniprot.org/core/title"S-Nitrosation of Arabidopsis thaliana Protein Tyrosine Phosphatase 1 Prevents Its Irreversible Oxidation by Hydrogen Peroxide."xsd:string
http://purl.uniprot.org/citations/35222471http://purl.uniprot.org/core/volume"13"xsd:string
http://purl.uniprot.org/citations/35222471http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/35222471
http://purl.uniprot.org/citations/35222471http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/35222471
http://purl.uniprot.org/uniprot/#_F4IA41-mappedCitation-35222471http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/35222471
http://purl.uniprot.org/uniprot/#_Q39023-mappedCitation-35222471http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/35222471
http://purl.uniprot.org/uniprot/#_Q39026-mappedCitation-35222471http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/35222471
http://purl.uniprot.org/uniprot/#_Q0WVS7-mappedCitation-35222471http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/35222471
http://purl.uniprot.org/uniprot/#_O82656-mappedCitation-35222471http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/35222471
http://purl.uniprot.org/uniprot/F4IA41http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/35222471