| http://purl.uniprot.org/citations/16376338 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16376338 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16376338 | http://www.w3.org/2000/01/rdf-schema#comment | "Recognition of phosphorylated serine/threonine-containing motifs by 14-3-3 depends on the dimerization of 14-3-3. However, the molecular cues that control 14-3-3 dimerization are not well understood. In order to identify proteins that control 14-3-3 dimerization, we analyzed proteins that have effects on 14-3-3 dimerization and report that protein kinase A (PKA) phosphorylates 14-3-3zeta at a specific residue (Ser58). Phosphorylation by PKA leads to modulation of 14-3-3zeta dimerization and affect its interaction with partner proteins. Substitution of Ser58 to Ala completely abolished phosphorylation of 14-3-3zeta by PKA. A phospho-mimic mutant of 14-3-3zeta, Ser58 to Glu substitution, failed to form homodimers, showed reduced interaction with 14-3-3epsilon and p53, and could not enhance transcriptional activity of p53. Moreover, activation of PKA decreases and inhibition of PKA increases the dimerization of 14-3-3zeta and the functional interaction of 14-3-3zeta with p53. Therefore, our results suggest that PKA is a new member of protein kinases that can phosphorylate and impair the function of 14-3-3."xsd:string |
| http://purl.uniprot.org/citations/16376338 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.febslet.2005.12.024"xsd:string |
| http://purl.uniprot.org/citations/16376338 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.febslet.2005.12.024"xsd:string |
| http://purl.uniprot.org/citations/16376338 | http://purl.uniprot.org/core/author | "Baek K.-H."xsd:string |
| http://purl.uniprot.org/citations/16376338 | http://purl.uniprot.org/core/author | "Baek K.-H."xsd:string |
| http://purl.uniprot.org/citations/16376338 | http://purl.uniprot.org/core/author | "Choi J.-K."xsd:string |
| http://purl.uniprot.org/citations/16376338 | http://purl.uniprot.org/core/author | "Choi J.-K."xsd:string |
| http://purl.uniprot.org/citations/16376338 | http://purl.uniprot.org/core/author | "Gu Y.-M."xsd:string |
| http://purl.uniprot.org/citations/16376338 | http://purl.uniprot.org/core/author | "Gu Y.-M."xsd:string |
| http://purl.uniprot.org/citations/16376338 | http://purl.uniprot.org/core/author | "Jin Y.-H."xsd:string |
| http://purl.uniprot.org/citations/16376338 | http://purl.uniprot.org/core/author | "Jin Y.-H."xsd:string |
| http://purl.uniprot.org/citations/16376338 | http://purl.uniprot.org/core/author | "Lee K.-Y."xsd:string |
| http://purl.uniprot.org/citations/16376338 | http://purl.uniprot.org/core/author | "Lee K.-Y."xsd:string |
| http://purl.uniprot.org/citations/16376338 | http://purl.uniprot.org/core/author | "Yeo C.-Y."xsd:string |
| http://purl.uniprot.org/citations/16376338 | http://purl.uniprot.org/core/author | "Yeo C.-Y."xsd:string |
| http://purl.uniprot.org/citations/16376338 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
| http://purl.uniprot.org/citations/16376338 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
| http://purl.uniprot.org/citations/16376338 | http://purl.uniprot.org/core/name | "FEBS Lett."xsd:string |
| http://purl.uniprot.org/citations/16376338 | http://purl.uniprot.org/core/name | "FEBS Lett."xsd:string |
| http://purl.uniprot.org/citations/16376338 | http://purl.uniprot.org/core/pages | "305-310"xsd:string |
| http://purl.uniprot.org/citations/16376338 | http://purl.uniprot.org/core/pages | "305-310"xsd:string |
| http://purl.uniprot.org/citations/16376338 | http://purl.uniprot.org/core/title | "Protein kinase A phosphorylates and regulates dimerization of 14-3-3 epsilon."xsd:string |
| http://purl.uniprot.org/citations/16376338 | http://purl.uniprot.org/core/title | "Protein kinase A phosphorylates and regulates dimerization of 14-3-3 epsilon."xsd:string |