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Tau local structure shields an amyloid-forming motif and controls aggregation propensity.

Abstract：

:Tauopathies are neurodegenerative diseases characterized by intracellular amyloid deposits of tau protein. Missense mutations in the tau gene (MAPT) correlate with aggregation propensity and cause dominantly inherited tauopathies, but their biophysical mechanism driving amyloid formation is poorly understood. Many disease-associated mutations localize within tau's repeat domain at inter-repeat interfaces proximal to amyloidogenic sequences, such as 306VQIVYK311. We use cross-linking mass spectrometry, recombinant protein and synthetic peptide systems, in silico modeling, and cell models to conclude that the aggregation-prone 306VQIVYK311 motif forms metastable compact structures with its upstream sequence that modulates aggregation propensity. We report that disease-associated mutations, isomerization of a critical proline, or alternative splicing are all sufficient to destabilize this local structure and trigger spontaneous aggregation. These findings provide a biophysical framework to explain the basis of early conformational changes that may underlie genetic and sporadic tau pathogenesis.

journal_name

Nat Commun

journal_title

Nature communications

authors

Chen D,Drombosky KW,Hou Z,Sari L,Kashmer OM,Ryder BD,Perez VA,Woodard DR,Lin MM,Diamond MI,Joachimiak LA

doi

10.1038/s41467-019-10355-1

subject

Has Abstract

pub_date

2019-06-07 00:00:00

pages

2493

issue

1

issn

2041-1723

pii

10.1038/s41467-019-10355-1

journal_volume

10

pub_type

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