Protein homeostasis is fundamental to cellular viability and relies on the precise folding and localization of proteins. Newly synthesized proteins are inherently vulnerable to misfolding and aggregation as a result of their amino acid sequences, cellular stress, and aging. Molecular chaperones play critical roles in promoting correct protein folding and regulating the trafficking of membrane proteins to their appropriate cellular destinations. Since protein misfolding and aggregation are toxic and central to the pathogenesis of numerous protein conformational diseases including neurodegenerative diseases, molecular chaperones represent compelling therapeutic targets.

Our research group combines biochemistry, protein engineering, and cell biology 1) to understand the mechanistic roles of molecular chaperones in maintaining protein homeostasis and 2) to design therapeutic chaperones for neurodegenerative diseases.

Specific research questions:

1. How do molecular chaperones counteract the pathological aggregates associated with neurodegenerative diseases?
2. Can we design therapeutic chaperones to eliminate pathological protein aggregates?
3. How do the cytosolic chaperone PEX19 mediate the delivery of peroxisomal membrane proteins to peroxisomes?
4. How is peroxisome dysfunction observed in the peroxisome biogenesis disorder linked to neurodegenerative diseases?