Jill L. Johnson, Ph.D.

Summary: Each protein has to be a particular three-dimensional shape to work properly, and misfolded proteins cause a range of diseases. My lab studies proteins in the cell that help other proteins fold. More specifically, the Hsp90 molecular chaperone, which help 15-20% of all proteins fold. Inhibitors against Hsp90 have promise to treat cancer, since many of the proteins that promote cancerous growth require Hsp90. However, they have negative side effects that limit their use. My lab uses a genetic approach in yeast to learn how Hsp90 mutation affects different proteins. The long term goal is to translate that into more specific inhibitors of Hsp90 that have fewer negative effects.

Minimum Classes: Genetics BIOL 310/315 or Biol 312 would be helpful, but not required.

Projects:

One project is to better understand how a cochaperone regulates Hsp90 function. We know that overexpression of the cochaperone has different effects on Hsp90 function. We want to develop new tools to allow us to turn off/on expression more rapidly. This will allow us to identify defects that happen most rapidly when Hsp90 is turned off.

Another project is to better characterize one of the dozens of proteins that require Hsp90 in order to understand how Hsp90 mutation affects its function. These proteins have diverse roles in cell signaling, splicing and cellular transport.