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Related Experiment Videos

Expanded polyglutamine stretches form an 'aggresome'.

Takayoshi Shimohata1, Aki Sato, James R Burke

  • 1Department of Neurology, Brain Research Institute, Niigata University, 1-757 Asahimachi, Niigata 951-8181, Japan.

Neuroscience Letters
|April 18, 2002
PubMed
Summary

Expanded polyglutamine (polyQ) proteins in dentatorubral-pallidoluysian atrophy (DRPLA) form aggresomes at the microtubule-organizing center. Disruption of microtubules causes aggregates to scatter, revealing their transport mechanism.

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Area of Science:

  • Neuroscience
  • Cell Biology
  • Molecular Biology

Background:

  • Polyglutamine (polyQ) diseases are a group of neurodegenerative disorders.
  • Dentatorubral-pallidoluysian atrophy (DRPLA) is a type of polyQ disease.
  • The formation and cellular localization of polyQ aggregates are key to disease pathogenesis.

Purpose of the Study:

  • To investigate the mechanisms of aggregate body formation in polyglutamine (polyQ) diseases.
  • To elucidate the role of microtubules in the cellular transport and localization of expanded polyQ proteins, using DRPLA as a model.

Main Methods:

  • Expression of truncated DRPLA protein with expanded polyQ stretches in COS-7 cells.
  • Co-localization studies with gamma-tubulin (microtubule-organizing center marker).

Related Experiment Videos

  • Assessment of vimentin network integrity.
  • Disruption of microtubules using nocodazole.

    • Main Results:

    • Expanded polyQ DRPLA protein forms perinuclear aggregate bodies co-localized with gamma-tubulin.
    • These aggregates are surrounded by a collapsed vimentin network.
    • Microtubule disruption leads to scattered, smaller aggregate bodies.
    • Evidence suggests aggregates move along microtubules to the MTOC.

    Conclusions:

    • Truncated DRPLA proteins with expanded polyQ stretches unfold and form peripheral aggregates.
    • These aggregates are transported via microtubules to the microtubule-organizing center (MTOC).
    • Aggregates accumulate at the MTOC as distinct 'aggresomes', contributing to DRPLA pathogenesis.