Tau oligomerization: A role for tau aggregation intermediates linked to neurodegeneration

N. Sahara, S. Maeda, A. Takashima

Research output: Contribution to journalReview articlepeer-review

68 Citations (Scopus)

Abstract

Intracellular accumulation of filamentous tau proteins is a defining feature of neurodegenerative diseases, including Alzheimer's disease, progressive supranuclear palsy, corticobasal degeneration, Pick's disease, and frontotemporal dementia with Parkinsonism linked to chromosome 17, all known collectively as tauopathies. Tau protein is a member of microtubule (MT)-associated proteins. Tau is a highly soluble and natively unfolded protein dominated by a random coil structure in solution. It is believed that aberrant modifications of tau, including phosphorylation, truncation, and conformational changes, induce filamentous aggregation. However, the mechanism underlying the conversion of tau protein from a soluble state to one of insoluble aggregates still remains elusive. The importance of tau aggregation intermediates (e.g. tau dimer, tau multimer, and granular tau oligomer) in disease pathogenesis was suggested by recent studies. Here, we review the latest developments in tracking the structural changes of tau protein and discuss the utility improving our understanding of tau aggregation pathway leading to human tauopathies.

Original languageEnglish
Pages (from-to)591-598
Number of pages8
JournalCurrent Alzheimer Research
Volume5
Issue number6
DOIs
Publication statusPublished - 2008 Dec 1
Externally publishedYes

Keywords

  • Aggregation intermediates
  • Alzheimer's disease
  • Atomic force microscopy
  • Granular tau oligomer
  • Tau
  • Tau dimer
  • Tau multimer
  • Tauopathy

ASJC Scopus subject areas

  • Neurology
  • Clinical Neurology

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