| http://purl.uniprot.org/citations/11956199 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11956199 | http://www.w3.org/2000/01/rdf-schema#comment | "Alpha-synuclein is the major component of Lewy bodies in patients with Parkinson's disease, and mutations in the alpha-synuclein gene are responsible for some familial forms of the disease. alpha-Synuclein is enriched in the presynapse, but its synaptic targets are unknown. Synphilin-1 associates in vivo with alpha-synuclein promoting the formation of intracellular inclusions. Additionally synphilin-1 has been found to be an intrinsic component of Lewy bodies in patients with Parkinson's disease. To understand the role of synphilin-1 in Parkinson's disease, we sought to define its localization and function in the brain. We now report that, like alpha-synuclein, synphilin-1 was enriched in neurons. In young rats, synphilin-1 was prominent in neuronal cell bodies but gradually migrated to neuropil during development. Immunoelectron microscopy of adult rat cerebral cortex demonstrated that synphilin-1 was highly enriched in presynaptic nerve terminals. Synphilin-1 co-immunoprecipitated with synaptic vesicles, indicating a strong association with these structures. In vitro binding experiments demonstrated that the N terminus of synphilin-1 robustly associated with synaptic vesicles and that this association was resistant to high salt washing but was abolished by inclusion of alpha-synuclein in the incubation medium. Our data indicated that synphilin-1 is a synaptic partner of alpha-synuclein, and it may mediate synaptic roles attributed to alpha-synuclein."xsd:string |
| http://purl.uniprot.org/citations/11956199 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m201115200"xsd:string |
| http://purl.uniprot.org/citations/11956199 | http://purl.uniprot.org/core/author | "Ross C.A."xsd:string |
| http://purl.uniprot.org/citations/11956199 | http://purl.uniprot.org/core/author | "Engelender S."xsd:string |
| http://purl.uniprot.org/citations/11956199 | http://purl.uniprot.org/core/author | "Carneiro K."xsd:string |
| http://purl.uniprot.org/citations/11956199 | http://purl.uniprot.org/core/author | "Menezes J.R."xsd:string |
| http://purl.uniprot.org/citations/11956199 | http://purl.uniprot.org/core/author | "Ribeiro C.S."xsd:string |
| http://purl.uniprot.org/citations/11956199 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
| http://purl.uniprot.org/citations/11956199 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/11956199 | http://purl.uniprot.org/core/pages | "23927-23933"xsd:string |
| http://purl.uniprot.org/citations/11956199 | http://purl.uniprot.org/core/title | "Synphilin-1 is developmentally localized to synaptic terminals, and its association with synaptic vesicles is modulated by alpha-synuclein."xsd:string |
| http://purl.uniprot.org/citations/11956199 | http://purl.uniprot.org/core/volume | "277"xsd:string |
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