A common feature of multiple neurodegenerative diseases is the formation large protein rich aggregates inside neurons. Accumulating evidence suggests that the build-up of these large aggregates, may be driven primarily by misfolded amyloid proteins. Our focus is to investigate how chaperones involved in regulation of protein folding and protein homeostasis, might suppress aggregation of amyloid proteins such as alpha-synuclein, ,tau and huntingtin. We are particularly interested in a class of HSP70 co-chaperones named DNAJ proteins. Mutations in several DNAJ genes are genetically linked to an increased risk of contracting Parkinson’s Disease, but very little is known about the molecular mechanisms behind this. Our research group uses a variety of molecular biology tools, cell culture models and rodent models to pinpoint how these DNAJ proteins may suppress protein aggregation and be neuroprotective in Parkinson’s Disease and other neurodegenerative diseases.