This presentation is accessible only to the Illinois State University community.

  • Off-Campus ISU Users: To download this item, click the "Off-Campus Download" button below. You will be prompted to log in with your ISU ULID and password.

Publication Date


Document Type


Degree Type



Biological Sciences


Alysia Vrailas-Mortimer

Mentor Department

Biological Sciences


As organisms age they accumulate misfolded and damaged protein that can lead to protein aggregation, which can be toxic and lead to a diseased state and eventual death of the cell. We have recently found that the p38 MAP Kinase (p38Kb) plays a major role in regulating protein aggregation in Drosophila melanogaster through its interaction with the Chaperone Assisted Selective Autophagy (CASA) complex. The CASA complex is a pathway that helps with the degradation of the misfolded and damaged proteins to prevent protein aggregation. The chaperone proteins in the complex refolds the proteins. The proteins that cannot be refolded are polyubiquitinated and are handed over to a protein called ref(2)p for degradation. We hypothesize that p38Kb binds to ref(2)p to help facilitate the handoff of the target protein for degradation. We have identified several regions in ref(2)p that p38Kb may bind to or phosphorylate. To understand the role that p38Kb plays in regulating the CASA complex and ref(2)p mediated protein degradation, we have made transgenic flies in which these different p38Kb sites are mutated in ref(2)p. The effects of these mutations in ref(2)p were analyzed using a western blot to see if the mutations could change the stability of ref(2)p. We find that certain mutations in ref(2 )p affects the detection and stability of the protein. In future studies we will use Coimmunoprecipitation experiments to test if these regions are important for binding between p38Kb and ref(2)p.

Off-Campus Download