Mechanisms of Toxicity in Huntington's Disease

Project Details

Huntington's disease is caused by dominant mutations in the Huntingtin gene.  The mutations lead the gene product, Huntingtin, to aggregate into visible inclusion bodies in neurons. We are interested in understanding the molecular basis for why the mutant proteins are toxic and how this relates to the physical process of aggregation.  We study cellular models of Huntington disease and apply a broad range of methods to measure the toxicity of the mutant Huntingtin gene product.

Our team has developed novel methods to measure precisely how the protein aggregates and tp separate cells that have the mutant protein aggregated at different stages of the aggregation process.  We are studying the changes in the cells as the protein aggregates.

Figure 1: Images of GFP-tagged Huntingtin aggregates (inclusions) that form inside cells.  Here we purified the inclusions and stained the surface proteins with an antibody for D-STORM super resolution imaging.  Images courtesy of Paul McMillan, Mikhail Trubetskov and Svenja Bolz.

Research Group

Hatters laboratory: Protein misfolding and proteostasis in neurodegenerative diseases



Faculty Research Themes

Neuroscience

School Research Themes

Biomedical Neuroscience, Cellular Imaging & Structural Biology



Key Contact

For further information about this research, please contact the research group leader.

Department / Centre

Biochemistry and Molecular Biology

Unit / Centre

Hatters laboratory: Protein misfolding and proteostasis in neurodegenerative diseases