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http://purl.uniprot.org/citations/26323479http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/26323479http://www.w3.org/2000/01/rdf-schema#comment"Extracellular α-synuclein (α-syn) assemblies can be up-taken by neurons; however, their interaction with the plasma membrane and proteins has not been studied specifically. Here we demonstrate that α-syn assemblies form clusters within the plasma membrane of neurons. Using a proteomic-based approach, we identify the α3-subunit of Na+/K+-ATPase (NKA) as a cell surface partner of α-syn assemblies. The interaction strength depended on the state of α-syn, fibrils being the strongest, oligomers weak, and monomers none. Mutations within the neuron-specific α3-subunit are linked to rapid-onset dystonia Parkinsonism (RDP) and alternating hemiplegia of childhood (AHC). We show that freely diffusing α3-NKA are trapped within α-syn clusters resulting in α3-NKA redistribution and formation of larger nanoclusters. This creates regions within the plasma membrane with reduced local densities of α3-NKA, thereby decreasing the efficiency of Na+ extrusion following stimulus. Thus, interactions of α3-NKA with extracellular α-syn assemblies reduce its pumping activity as its mutations in RDP/AHC."xsd:string
http://purl.uniprot.org/citations/26323479http://purl.org/dc/terms/identifier"doi:10.15252/embj.201591397"xsd:string
http://purl.uniprot.org/citations/26323479http://purl.uniprot.org/core/author"Melki R."xsd:string
http://purl.uniprot.org/citations/26323479http://purl.uniprot.org/core/author"Almeida L.G."xsd:string
http://purl.uniprot.org/citations/26323479http://purl.uniprot.org/core/author"Aperia A."xsd:string
http://purl.uniprot.org/citations/26323479http://purl.uniprot.org/core/author"Redeker V."xsd:string
http://purl.uniprot.org/citations/26323479http://purl.uniprot.org/core/author"Bousset L."xsd:string
http://purl.uniprot.org/citations/26323479http://purl.uniprot.org/core/author"Triller A."xsd:string
http://purl.uniprot.org/citations/26323479http://purl.uniprot.org/core/author"Fritz N."xsd:string
http://purl.uniprot.org/citations/26323479http://purl.uniprot.org/core/author"Renner M."xsd:string
http://purl.uniprot.org/citations/26323479http://purl.uniprot.org/core/author"Lena C."xsd:string
http://purl.uniprot.org/citations/26323479http://purl.uniprot.org/core/author"Pieri L."xsd:string
http://purl.uniprot.org/citations/26323479http://purl.uniprot.org/core/author"Shrivastava A.N."xsd:string
http://purl.uniprot.org/citations/26323479http://purl.uniprot.org/core/author"Liebmann T."xsd:string
http://purl.uniprot.org/citations/26323479http://purl.uniprot.org/core/author"Spolidoro M."xsd:string
http://purl.uniprot.org/citations/26323479http://purl.uniprot.org/core/date"2015"xsd:gYear
http://purl.uniprot.org/citations/26323479http://purl.uniprot.org/core/name"EMBO J"xsd:string
http://purl.uniprot.org/citations/26323479http://purl.uniprot.org/core/pages"2408-2423"xsd:string
http://purl.uniprot.org/citations/26323479http://purl.uniprot.org/core/title"alpha-synuclein assemblies sequester neuronal alpha3-Na+/K+-ATPase and impair Na+ gradient."xsd:string
http://purl.uniprot.org/citations/26323479http://purl.uniprot.org/core/volume"34"xsd:string
http://purl.uniprot.org/citations/26323479http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/26323479
http://purl.uniprot.org/citations/26323479http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/26323479
http://purl.uniprot.org/uniprot/#_B3KSY7-mappedCitation-26323479http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/26323479
http://purl.uniprot.org/uniprot/#_A0A2Z5HU10-mappedCitation-26323479http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/26323479