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In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein
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RNA stores tau reversibly in complex coacervates.

Xuemei Zhang1,2, Yanxian Lin3, Neil A Eschmann4

  • 1Molecular, Cell and Developmental Biology, University of California Santa Barbara, Santa Barbara, California, United States of America.

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Tau protein forms liquid droplets via liquid-liquid phase separation (LLPS) with tRNAs, a process sensitive to salt and temperature. This droplet state may predispose tau to form neurodegenerative fibrils.

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Neuroscience

Background:

  • Nonmembrane-bound organelles acting as liquid droplets are crucial in eukaryotic cells.
  • Dysregulation of these droplets is linked to neurodegenerative diseases.

Purpose of the Study:

  • To investigate the biophysical properties of tau protein, a key component of Alzheimer's neurofibrillary tangles.
  • To determine if tau can undergo liquid-liquid phase separation (LLPS) and form liquid droplets in cells.

Main Methods:

  • Studied tau protein's ability to form liquid droplets in the presence of RNA, specifically transfer RNAs (tRNAs).
  • Investigated the influence of salt concentration and temperature on tau droplet formation.
  • Assessed changes in tau conformation and aggregation propensity within the droplet state using biophysical assays.

Main Results:

  • Tau protein forms liquid droplets through LLPS with tRNAs, exhibiting characteristics of complex coacervation.
  • The LLPS process is modulated by salt concentration and temperature, indicating electrostatic and entropic influences.
  • Tau within droplets remains dynamic, but prolonged residence can lead to the formation of aggregation-prone β-sheet structures.

Conclusions:

  • Tau protein can undergo LLPS, forming dynamic liquid droplets with tRNAs.
  • The cellular droplet state may act as a precursor, promoting tau aggregation and the development of neurodegenerative pathologies.