Alpha-synuclein and tau: teammates in neurodegeneration?

Simon Moussaud, Daryl R. Jones, Elisabeth L. Moussaud-Lamodière, Marion Delenclos, Owen A Ross, Pamela J McLean

Research output: Contribution to journalArticle

93 Scopus citations

Abstract

The accumulation of α-synuclein aggregates is the hallmark of Parkinson's disease, and more generally of synucleinopathies. The accumulation of tau aggregates however is classically found in the brains of patients with dementia, and this type of neuropathological feature specifically defines the tauopathies. Nevertheless, in numerous cases α-synuclein positive inclusions are also described in tauopathies and vice versa, suggesting a co-existence or crosstalk of these proteinopathies. Interestingly, α-synuclein and tau share striking common characteristics suggesting that they may work in concord. Tau and α-synuclein are both partially unfolded proteins that can form toxic oligomers and abnormal intracellular aggregates under pathological conditions. Furthermore, mutations in either are responsible for severe dominant familial neurodegeneration. Moreover, tau and α-synuclein appear to promote the fibrillization and solubility of each other in vitro and in vivo. This suggests that interactions between tau and α-synuclein form a deleterious feed-forward loop essential for the development and spreading of neurodegeneration. Here, we review the recent literature with respect to elucidating the possible links between α-synuclein and tau.

Original languageEnglish (US)
Pages (from-to)43
Number of pages1
JournalMolecular Neurodegeneration
Volume9
DOIs
StatePublished - 2014

ASJC Scopus subject areas

  • Medicine(all)

Fingerprint Dive into the research topics of 'Alpha-synuclein and tau: teammates in neurodegeneration?'. Together they form a unique fingerprint.

  • Cite this