α-synuclein assemblies sequester neuronal α3-Na+/K+-ATPase and impair Na+ gradient.
Identifieur interne : 000279 ( PubMed/Corpus ); précédent : 000278; suivant : 000280α-synuclein assemblies sequester neuronal α3-Na+/K+-ATPase and impair Na+ gradient.
Auteurs : Amulya Nidhi Shrivastava ; Virginie Redeker ; Nicolas Fritz ; Laura Pieri ; Leandro G. Almeida ; Maria Spolidoro ; Thomas Liebmann ; Luc Bousset ; Marianne Renner ; Clément Léna ; Anita Aperia ; Ronald Melki ; Antoine TrillerSource :
- The EMBO journal [ 1460-2075 ] ; 2015.
English descriptors
- KwdEn :
- Hemiplegia (genetics), Hemiplegia (metabolism), Hemiplegia (pathology), Humans, Multiprotein Complexes (genetics), Multiprotein Complexes (metabolism), Mutation, Neurons (metabolism), Neurons (pathology), Parkinsonian Disorders (genetics), Parkinsonian Disorders (metabolism), Parkinsonian Disorders (pathology), Sodium-Potassium-Exchanging ATPase (genetics), Sodium-Potassium-Exchanging ATPase (metabolism), alpha-Synuclein (genetics), alpha-Synuclein (metabolism).
- MESH :
- chemical , genetics : Multiprotein Complexes, Sodium-Potassium-Exchanging ATPase, alpha-Synuclein.
- genetics : Hemiplegia, Parkinsonian Disorders.
- metabolism : Hemiplegia, Multiprotein Complexes, Neurons, Parkinsonian Disorders, Sodium-Potassium-Exchanging ATPase, alpha-Synuclein.
- pathology : Hemiplegia, Neurons, Parkinsonian Disorders.
- Humans, Mutation.
Abstract
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.
DOI: 10.15252/embj.201591397
PubMed: 26323479
Links to Exploration step
pubmed:26323479Le document en format XML
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<front><div type="abstract" xml:lang="en">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.</div>
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<Abstract><AbstractText>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.</AbstractText>
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