| http://purl.uniprot.org/citations/14645218 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/14645218 | http://www.w3.org/2000/01/rdf-schema#comment | "Alpha-synuclein is a phosphoprotein that accumulates as a major component of Lewy bodies in the brains of patients with Parkinson disease. Synphilin-1, which is also present in Lewy bodies, binds with alpha-synuclein and forms cytoplasmic inclusions in transfected cells. Yet the molecular determinants of this protein-protein interaction are unknown. Here we report that casein kinase II (CKII) phosphorylates synphilin-1 and that the beta subunit of this enzyme complex binds to synphilin-1. Additionally, both CKII alpha and beta subunits are present within cytoplasmic inclusions in cells that overexpress synphilin-1. Notably, the interaction between synphilin-1 and alpha-synuclein is markedly dependent on phosphorylation. Inhibition of CKII activity by 5,6-dichloro-1-beta-D-ribofuranosylbenzimidazole blocks the binding between these two proteins and significantly reduces the percentage of cells that contain eosinophilic cytoplasmic inclusions. Mutation of the major CKII phosphorylation site in alpha-synuclein (S129A) has no significant impact on the binding between alpha-synuclein and synphilin-1 or on the formation of synphilin-1/alpha-synuclein-positive inclusions. These data suggest that the CKII-mediated phosphorylation of synphilin-1 rather than that of alpha-synuclein is critical in modulating their tendency to aggregate into inclusions. These observations collectively indicate that a ubiquitous post-translational modification such as phosphorylation can regulate inclusion body formation in the context of alpha-synuclein and synphilin-1 interaction."xsd:string |
| http://purl.uniprot.org/citations/14645218 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m312760200"xsd:string |
| http://purl.uniprot.org/citations/14645218 | http://purl.uniprot.org/core/author | "Lee G."xsd:string |
| http://purl.uniprot.org/citations/14645218 | http://purl.uniprot.org/core/author | "Lee S.S."xsd:string |
| http://purl.uniprot.org/citations/14645218 | http://purl.uniprot.org/core/author | "Lee S.H."xsd:string |
| http://purl.uniprot.org/citations/14645218 | http://purl.uniprot.org/core/author | "Park K."xsd:string |
| http://purl.uniprot.org/citations/14645218 | http://purl.uniprot.org/core/author | "Tanaka M."xsd:string |
| http://purl.uniprot.org/citations/14645218 | http://purl.uniprot.org/core/author | "Kim Y.M."xsd:string |
| http://purl.uniprot.org/citations/14645218 | http://purl.uniprot.org/core/author | "Mouradian M.M."xsd:string |
| http://purl.uniprot.org/citations/14645218 | http://purl.uniprot.org/core/author | "Junn E."xsd:string |
| http://purl.uniprot.org/citations/14645218 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/14645218 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/14645218 | http://purl.uniprot.org/core/pages | "6834-6839"xsd:string |
| http://purl.uniprot.org/citations/14645218 | http://purl.uniprot.org/core/title | "Casein kinase II-mediated phosphorylation regulates alpha-synuclein/synphilin-1 interaction and inclusion body formation."xsd:string |
| http://purl.uniprot.org/citations/14645218 | http://purl.uniprot.org/core/volume | "279"xsd:string |
| http://purl.uniprot.org/citations/14645218 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/14645218 |
| http://purl.uniprot.org/citations/14645218 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/14645218 |
| http://purl.uniprot.org/uniprot/#_A6KTU1-mappedCitation-14645218 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/14645218 |
| http://purl.uniprot.org/uniprot/#_A6KTU4-mappedCitation-14645218 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/14645218 |
| http://purl.uniprot.org/uniprot/#_A0A1U9X7J2-mappedCitation-14645218 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/14645218 |
| http://purl.uniprot.org/uniprot/#_A0A8L2UP98-mappedCitation-14645218 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/14645218 |
| http://purl.uniprot.org/uniprot/#_A0A2Z5HTN7-mappedCitation-14645218 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/14645218 |
| http://purl.uniprot.org/uniprot/#_A0A2Z5HU10-mappedCitation-14645218 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/14645218 |
| http://purl.uniprot.org/uniprot/#_B3KMP8-mappedCitation-14645218 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/14645218 |