Cellular proteins are composed of long chains of amino acids which, when assembled, will fold into complicated, three-dimensional shapes. The ultimate shape of each protein suits it to carry out its particular cell functions, and therefore, it is imperative that each protein is properly folded. Various cell stresses, such as the accumulation of oxidizing species (oxidative stress), can damage these amino acids, and prevent proteins from folding correctly. As such, cells contain elaborate mechanisms which serve to mitigate the damage done to folding proteins. Two such mechanisms center around the proteins IRE1 and PDI. IRE1 is known to sense the accumulation of damaged proteins in the endoplasmic reticulum, and in response to high levels of damaged proteins, IRE1 signals the upregulation of proteins that can assist the cell in folding these damaged proteins. PDI is involved in activating and deactivating the enzyme Ero1, which is the primary generator of oxidizing species in the endoplasmic reticulum. In both cases, the detailed mechanisms that allow these proteins to sense and respond to stimuli are not fully understood. Our aim is to elucidate the intricacies of these signaling mechanisms so that we can better understand how misregulation of these proteins can manifest in various protein-folding diseases. Interested students should contact Professor Siegenthaler. No prior biochemistry or molecular biology experience is necessary.
Completion of Chem 102 or Chem 111.
Number of Student Researchers
Applications open on 01/03/2021 and close on 03/22/2021