Clustering of Tau fibrils impairs the synaptic composition of α3-Na⁺/K⁺-ATPase and AMPA receptors.

ABSTRACT: Tau assemblies have prion-like properties: they propagate from one neuron to another and amplify by seeding the aggregation of endogenous Tau. Although key in prion-like propagation, the binding of exogenous Tau assemblies to the plasma membrane of naïve neurons is not understood. We report that fibrillar Tau forms clusters at the plasma membrane following lateral diffusion. We found that the fibrils interact with the Na⁺/K⁺-ATPase (NKA) and AMPA receptors. The consequence of the clustering is a reduction in the amount of α3-NKA and an increase in the amount of GluA2-AMPA receptor at synapses. Furthermore, fibrillar Tau destabilizes functional NKA complexes. Tau and α-synuclein aggregates often co-exist in patients' brains. We now show evidences for cross-talk between

SUBMITTER: Shrivastava AN 

PROVIDER: S-EPMC6356061 | biostudies-literature | 2019 Feb

REPOSITORIES: biostudies-literature