http://purl.uniprot.org/citations/19919952 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/19919952 | http://www.w3.org/2000/01/rdf-schema#comment | "Protein tyrosine phosphatase (PTP)-PEST is expressed in a wide variety of several cell types and is an efficient regulator of cell adhesion, spreading and migration. PTP-PEST-associating molecules are important in elucidating the function of PTP-PEST. Herein, we have identified protein phosphatase 1alpha (PP1alpha) as a novel PTP-PEST binding protein, and then we aimed to determine how PP1alpha contributes to the phosphorylation at Ser39 of PTP-PEST, whose phosphorylation suppresses PTP-PEST enzymatic activity. The HEK 293 cells overexpressing exogenous PTP-PEST were stimulated by 12-O-tetradecanoylphorbol 13-acetate (TPA) and the phosphorylation of PTP-PEST at Ser39 was evaluated using an anti-phospho-Ser39 PTP-PEST specific antibody (anti-pS39-PEST Ab). It was demonstrated that the phosphorylation at Ser39 detected by anti-pS39-PEST Ab was dependent on TPA treatment and a significant inverse correlation between the PTP activity of PTP-PEST and anti-pS39-PEST Ab-immunoreactive band intensity. The phosphorylation of Ser39 was suppressed by co-transfection of a plasmid encoding wild-type PP1alpha, but not by that of the dominant-negative PP1alpha mutant. Furthermore, TPA-induced phosphorylation could take place in PTP-PEST catalytic domain, but the phosphorylation of PTP-PEST catalytic domain could not be abrogated by co-transfection of a plasmid expressing wild-type PP1alpha. In conclusion, PP1alpha associates with the non-catalytic domain of PTP-PEST and regulates PTP activity via dephosphorylation of phospho-Ser39."xsd:string |
http://purl.uniprot.org/citations/19919952 | http://purl.org/dc/terms/identifier | "doi:10.1093/jb/mvp191"xsd:string |
http://purl.uniprot.org/citations/19919952 | http://purl.uniprot.org/core/author | "Nakamura K."xsd:string |
http://purl.uniprot.org/citations/19919952 | http://purl.uniprot.org/core/author | "Mashima K."xsd:string |
http://purl.uniprot.org/citations/19919952 | http://purl.uniprot.org/core/author | "Ozawa T."xsd:string |
http://purl.uniprot.org/citations/19919952 | http://purl.uniprot.org/core/author | "Palmer H.E."xsd:string |
http://purl.uniprot.org/citations/19919952 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
http://purl.uniprot.org/citations/19919952 | http://purl.uniprot.org/core/name | "J Biochem"xsd:string |
http://purl.uniprot.org/citations/19919952 | http://purl.uniprot.org/core/pages | "493-500"xsd:string |
http://purl.uniprot.org/citations/19919952 | http://purl.uniprot.org/core/title | "Protein phosphatase 1alpha associates with protein tyrosine phosphatase-PEST inducing dephosphorylation of phospho-serine 39."xsd:string |
http://purl.uniprot.org/citations/19919952 | http://purl.uniprot.org/core/volume | "147"xsd:string |
http://purl.uniprot.org/citations/19919952 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/19919952 |
http://purl.uniprot.org/citations/19919952 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/19919952 |
http://purl.uniprot.org/uniprot/#_A0A140VJS9-mappedCitation-19919952 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/19919952 |
http://purl.uniprot.org/uniprot/#_C0STL0-mappedCitation-19919952 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/19919952 |
http://purl.uniprot.org/uniprot/#_C4TNW5-mappedCitation-19919952 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/19919952 |
http://purl.uniprot.org/uniprot/#_C4TNW6-mappedCitation-19919952 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/19919952 |
http://purl.uniprot.org/uniprot/#_B3KXM2-mappedCitation-19919952 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/19919952 |
http://purl.uniprot.org/uniprot/#_B4E105-mappedCitation-19919952 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/19919952 |
http://purl.uniprot.org/uniprot/#_Q16128-mappedCitation-19919952 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/19919952 |
http://purl.uniprot.org/uniprot/#_Q16129-mappedCitation-19919952 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/19919952 |
http://purl.uniprot.org/uniprot/#_P62136-mappedCitation-19919952 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/19919952 |
http://purl.uniprot.org/uniprot/#_Q05209-mappedCitation-19919952 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/19919952 |
http://purl.uniprot.org/uniprot/A0A140VJS9 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/19919952 |