Mechanistic study on the interaction between heat shock protein 90 and its chaperone p23

Many cancers overexpress the aryl hydrocarbon receptor (AhR) protein, which is a xenobiotic-sensitive signaling molecule involved in many diseases such as autoimmune diseases, stem cell differentiation, diabetes, and asthma. Currently, we have very limited understanding of the molecular mechanisms explaining how the stable state level of AhR is maintained in a cell. Previously, our lab has shown that reduction of the p23 protein, which is a component of the AhR cytoplasmic complex, causes an increase in degradation of the AhR protein. Exogenous p23 restores this phenotype, clearly showing that p23 is important in controlling AhR protein degradation. It is well established that p23 interacts directly with heat shock protein 90 (Hsp90). We hypothesize that the mechanism of how p23 regulates AhR protein degradation is Hsp90-dependent. This poster focuses on the requirement of p23 to interact with Hsp90