| http://purl.uniprot.org/citations/10601328 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10601328 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10601328 | http://www.w3.org/2000/01/rdf-schema#comment | "Protein tyrosine phosphatase PTP-SL retains mitogen-activated protein (MAP) kinases in the cytoplasm in an inactive form by association through a kinase interaction motif (KIM) and tyrosine dephosphorylation. The related tyrosine phosphatases PTP-SL and STEP were phosphorylated by the cAMP-dependent protein kinase A (PKA). The PKA phosphorylation site on PTP-SL was identified as the Ser(231) residue, located within the KIM. Upon phosphorylation of Ser(231), PTP-SL binding and tyrosine dephosphorylation of the MAP kinases extracellular signal-regulated kinase (ERK)1/2 and p38alpha were impaired. Furthermore, treatment of COS-7 cells with PKA activators, or overexpression of the Calpha catalytic subunit of PKA, inhibited the cytoplasmic retention of ERK2 and p38alpha by wild-type PTP-SL, but not by a PTP-SL S231A mutant. These findings support the existence of a novel mechanism by which PKA may regulate the activation and translocation to the nucleus of MAP kinases."xsd:string |
| http://purl.uniprot.org/citations/10601328 | http://purl.org/dc/terms/identifier | "doi:10.1083/jcb.147.6.1129"xsd:string |
| http://purl.uniprot.org/citations/10601328 | http://purl.org/dc/terms/identifier | "doi:10.1083/jcb.147.6.1129"xsd:string |
| http://purl.uniprot.org/citations/10601328 | http://purl.uniprot.org/core/author | "Torres J."xsd:string |
| http://purl.uniprot.org/citations/10601328 | http://purl.uniprot.org/core/author | "Torres J."xsd:string |
| http://purl.uniprot.org/citations/10601328 | http://purl.uniprot.org/core/author | "Pulido R."xsd:string |
| http://purl.uniprot.org/citations/10601328 | http://purl.uniprot.org/core/author | "Pulido R."xsd:string |
| http://purl.uniprot.org/citations/10601328 | http://purl.uniprot.org/core/author | "Blanco-Aparicio C."xsd:string |
| http://purl.uniprot.org/citations/10601328 | http://purl.uniprot.org/core/author | "Blanco-Aparicio C."xsd:string |
| http://purl.uniprot.org/citations/10601328 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
| http://purl.uniprot.org/citations/10601328 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
| http://purl.uniprot.org/citations/10601328 | http://purl.uniprot.org/core/name | "J. Cell Biol."xsd:string |
| http://purl.uniprot.org/citations/10601328 | http://purl.uniprot.org/core/name | "J. Cell Biol."xsd:string |
| http://purl.uniprot.org/citations/10601328 | http://purl.uniprot.org/core/pages | "1129-1136"xsd:string |
| http://purl.uniprot.org/citations/10601328 | http://purl.uniprot.org/core/pages | "1129-1136"xsd:string |
| http://purl.uniprot.org/citations/10601328 | http://purl.uniprot.org/core/title | "A novel regulatory mechanism of MAP kinases activation and nuclear translocation mediated by PKA and the PTP-SL tyrosine phosphatase."xsd:string |
| http://purl.uniprot.org/citations/10601328 | http://purl.uniprot.org/core/title | "A novel regulatory mechanism of MAP kinases activation and nuclear translocation mediated by PKA and the PTP-SL tyrosine phosphatase."xsd:string |
| http://purl.uniprot.org/citations/10601328 | http://purl.uniprot.org/core/volume | "147"xsd:string |
| http://purl.uniprot.org/citations/10601328 | http://purl.uniprot.org/core/volume | "147"xsd:string |
| http://purl.uniprot.org/citations/10601328 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/10601328 |
| http://purl.uniprot.org/citations/10601328 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/10601328 |
| http://purl.uniprot.org/citations/10601328 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/10601328 |
| http://purl.uniprot.org/citations/10601328 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/10601328 |