Proteomics,Multiomics

Dataset Information

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Identification of proteins interacting with extracellularly applied α-syn assemblies, Condition 3 - biological replicates (6/8)


ABSTRACT: Fibrillar α-Synuclein (α-Syn) is the principal component of Lewy bodies which are evident in individuals affected by Parkinson disease (PD). This neuropathologic form of α-Syn contributes to PD progression and propagation of exogeneous α-Syn between neurons has been demonstrated. In order to identify proteins interacting with extracellularly applied α-syn assemblies (either oligomeric or fibrillar α -syn) and identify in particular plasma membrane proteins exposed extracellularly, we exposed pure-neuronal cultures to oligomeric and fibrillar α-syn for 10 min, pulled down the complex, and identified the associated proteins using a proteomic-based approach. Using pull-down of whole cell lysates and MS, we have identified proteins interacting with extracellularly applied α-syn in three different conditions. Each condition consisted in three experimental replicates of cells exposed 10 min to α-syn assemblies and the non-treated cells used as controls.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Rattus Norvegicus (rat)

TISSUE(S): Brain, Astrocyte

DISEASE(S): Parkinson's Disease

SUBMITTER: Virginie Redeker  

LAB HEAD: Virginie Redeker; Ronald Melki

PROVIDER: PXD002261 | Pride | 2015-09-07

REPOSITORIES: Pride

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Publications


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,  ...[more]

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