Authors: Joshua Evans, Allison Voyles, McKenzie Bellon, Julianne Grose
Mentors: Julianne Grose
Insitution: Brigham Young University
Alpha-crystallin B (CryAB) is a small heat shock protein that acts as a molecular chaperone and plays an essential role in cytoskeletal organization and myofibril function. Human mutations in CryAB have been associated with various diseases, such as cardiomyopathy and cataracts. However, the precise molecular pathways and protein substrates of CryAB are not yet fully understood and require further investigation. This project aims to increase understanding of CryAB by determining proteins that bind wild-type versus disease-causing variants using yeast two-hybrid screens. It also involves testing for binding specificity of variant-binding partners. A series of these Y2H screens gives valuable information regarding the binding patterns of CryAB, showing distinct binding partners for different alleles of CryAB. Overall, the project provides greater insight into the molecular functions of CryAB as well as a better understanding of the dysfunctional pathways of its disease-causing variants—a factor which may, in the future, have potential applications to the treatment of related diseases in a clinical setting