The structure and phase of tau: from monomer to amyloid filament

Tau is a microtubule-associated protein involved in regulation of assembly and spatial organization of microtubule in neurons. However, in pathological conditions, tau monomers assemble into amyloid filaments characterized by the cross-β structures in a number of neurodegenerative diseases known as...

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Bibliographic Details
Published in:Cellular and molecular life sciences : CMLS 2021-03, Vol.78 (5), p.1873-1886
Main Authors: Zeng, Yifan, Yang, Jing, Zhang, Bailing, Gao, Meng, Su, Zhengding, Huang, Yongqi
Format: Article
Language:English
Subjects:
Alzheimer Disease - genetics
Alzheimer Disease - metabolism
Alzheimer's disease
Amino acids
Amyloid - chemistry
Amyloid - genetics
Amyloid - metabolism
Amyloidogenic Proteins - chemistry
Amyloidogenic Proteins - genetics
Amyloidogenic Proteins - metabolism
Animals
Assembly
Biochemistry
Biomedical and Life Sciences
Biomedicine
Cell Biology
Filaments
Heterogeneity
Humans
Intrinsically Disordered Proteins - chemistry
Intrinsically Disordered Proteins - genetics
Intrinsically Disordered Proteins - metabolism
Kinases
Laboratories
Life Sciences
Monomers
Mutation
Neurodegenerative diseases
NMR
Nuclear magnetic resonance
Phosphorylation
Post-translation
Protein Aggregation, Pathological
Protein Processing, Post-Translational
Proteins
Review
Tau protein
tau Proteins - chemistry
tau Proteins - genetics
tau Proteins - metabolism
Tauopathies - genetics
Tauopathies - metabolism
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Description
Summary:Tau is a microtubule-associated protein involved in regulation of assembly and spatial organization of microtubule in neurons. However, in pathological conditions, tau monomers assemble into amyloid filaments characterized by the cross-β structures in a number of neurodegenerative diseases known as tauopathies. In this review, we summarize recent progression on the characterization of structures of tau monomer and filament, as well as the dynamic liquid droplet assembly. Our aim is to reveal how post-translational modifications, amino acid mutations, and interacting molecules modulate the conformational ensemble of tau monomer, and how they accelerate or inhibit tau assembly into aggregates. Structure-based aggregation inhibitor design is also discussed in the context of dynamics and heterogeneity of tau structures.
ISSN:1420-682X
1420-9071
DOI:10.1007/s00018-020-03681-x