Molecular chaperone networks are crucial for the maintenance of cellular homeostasis. The molecular chaperones and their associated co-chaperones mediate vital roles in the cell including the functional maturation and assembly of client proteins; the folding of newly synthesized polypeptides; translocation through membranes; the prevention of aggregation; and the promotion of degradation of misfolded or non-native substrates by the ubiquitin proteasome system (UPS). My research programme, in the Molecular and Cellular Neuroscience laboratory, is focused on the imbalance of protein folding and degradation as an underlying mechanism of retinal degeneration and neurodegeneration. Our studies have characterized a unique proteostasis network in the specialized neuronal photoreceptors of the retina that integrates molecular chaperone mediated protein folding and proteasome mediated protein degradation to regulate photoreceptor-specific protein homeostasis. Dysfunction of this system causes the earliest and most severe form of retinal degeneration. Our studies have also revealed the functional importance of novel components of the cellular protein degradation systems not only in retinal degeneration, but also neurodegenerative disorders such as Alzheimer’s disease. We are interested in the functional characterization of these protein folding and degradation mechanisms and their overlap in other neurodegenerative diseases, including polyglutamine expansion diseases (Huntington’s disease and spinocerebellar ataxia type 3) and Parkinson’s disease.