Proper protein homeostasis is essential to all cells and requires the correct folding and localization. Due to the nature of amino acid sequences, environmental stress, and aging, newly synthesized proteins constantly face a risk of misfolding and aggregation in the cytosol before safely reaching their functional conformation and final destination. Cytosolic chaperones not only assist in the proper folding of soluble proteins but also fine-tune the influx of membrane proteins to their correct destination. Since protein aggregation and misfolding are toxic to the cells and are the common cause of numerous protein conformational diseases, molecular chaperones have been suggested as an excellent therapeutic target for those diseases.

Our research group combines biochemistry, protein engineering, and cell biology to understand the mechanistic roles of molecular chaperones in maintaining protein homeostasis and to design therapeutic chaperones for protein conformational diseases.
We will specifically ask the following main questions:
First, how can cytosolic chaperones counteract the pathological aggregates for neurodegenerative diseases?
Second, can we design therapeutic chaperones to remove pathological protein aggregates?
Third, how can a cytosolic chaperone deliver peroxisomal membrane proteins to the peroxisome?
Fourth, how can peroxisome dysfunction observed in the peroxisome biogenesis disorder be linked to neurodegenerative diseases?