Jason C. Young
🏢 Bellini Life Sciences Building, Room 457
🔬 Research interest: chaperones, heat shock proteins, protein folding, protein degradation, intracellular trafficking, endoplasmic reticulum, protein misfolding diseases
Protein misfolding underlies many diseases. These include genetic diseases of ion channels such as CFTR in cystic fibrosis and hERG in long QT syndrome, as well as neurodegeneration and cancer. Dr. Young’s research studies molecular chaperones, which are key factors in cellular protein folding and quality control. They aim to understand how the biochemical mechanisms of the major chaperone Hsp70 and its regulatory co-chaperones underlie their cellular functions. A central idea is that the co-chaperones determine the specificity of Hsp70 function. Using a combination of cell biology and pure protein biochemistry, the laboratory addresses how the Hsp70 system controls the balance between folding, trafficking and proteasomal degradation of misfolded ion channels and other proteins. Also, the lab is investigating the molecular mechanisms of protein refolding and disaggregation by Hsp70, and its potential as a therapeutic drug target in certain cancers.