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The interaction of α-synuclein and Tau: A molecular conspiracy in neurodegeneration?

Authors
  • Yan, Xu1
  • Uronen, Riikka-Liisa1
  • Huttunen, Henri J2
  • 1 Neuroscience Center, Helsinki Institute of Life Science (HiLIFE), University of Helsinki, 00014 Helsinki, Finland. , (Finland)
  • 2 Neuroscience Center, Helsinki Institute of Life Science (HiLIFE), University of Helsinki, 00014 Helsinki, Finland. Electronic address: [email protected] , (Finland)
Type
Published Article
Journal
Seminars in Cell and Developmental Biology
Publisher
Elsevier
Publication Date
Mar 01, 2020
Volume
99
Pages
55–64
Identifiers
DOI: 10.1016/j.semcdb.2018.05.005
PMID: 29738880
Source
Medline
Keywords
Language
English
License
Unknown

Abstract

α-synuclein and Tau are proteins prone to pathological misfolding and aggregation that are normally found in the presynaptic and axonal compartments of neurons. Misfolding initiates a homo-oligomerization and aggregation cascade culminating in cerebral accumulation of aggregated α-synuclein and Tau in insoluble protein inclusions in multiple neurodegenerative diseases. Traditionally, α-synuclein-containing Lewy bodies have been associated with Parkinson's disease and Tau-containing neurofibrillary tangles with Alzheimer's disease and various frontotemporal dementia syndromes. However, there is significant overlap and co-occurrence of α-synuclein and Tau pathologies in a spectrum of neurodegenerative diseases. Importantly, α-synuclein and Tau can interact in cells, and their pathological conformations are capable of templating further misfolding and aggregation of each other. They also share a number of protein interactors indicating that network perturbations may contribute to chronic proteotoxic stress and neuronal dysfunction in synucleinopathies and tauopathies, some of which share similarities in both neuropathological and clinical manifestations. In this review, we focus on the protein interactions of these two pathologically important proteins and consider a network biology perspective towards neurodegenerative diseases. Copyright © 2018 Elsevier Ltd. All rights reserved.

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