Polyglutamine expansion accelerates the dynamics of ataxin-1 and does not result in aggregate formation.

ABSTRACT:

Background

Polyglutamine expansion disorders are caused by an expansion of the polyglutamine (polyQ) tract in the disease related protein, leading to severe neurodegeneration. All polyQ disorders are hallmarked by the presence of intracellular aggregates containing the expanded protein in affected neurons. The polyQ disorder SpinoCerebellar Ataxia 1 (SCA1) is caused by a polyQ-expansion in the ataxin-1 protein, which is thought to lead to nuclear aggregates.

Methodology/principal findings

Using advanced live cell fluorescence microscopy and a filter retardation assay we show that nuclear accumulations formed by polyQ-expanded ataxin-1 do not resemble aggregates of other polyQ-expanded proteins. Instead of being static, insoluble aggregates, nuclear accumulations formed by th

SUBMITTER: Krol HA 

PROVIDER: S-EPMC2200796 | biostudies-literature | 2008 Jan

REPOSITORIES: biostudies-literature