Investigating the Role of Ras-like GTPases in TORC2 Localization of Saccharomyces cerevisiae

Summer 2017

Iris Li : Molecular & Cell Biology

Donor: Pergo Fund
Mentor: Jeremy Thorner

The Target of Rapamycin (TOR) is a protein kinase involved in many aspects of cell physiology. Because of its importance in regulating growth, TOR has been central to metabolic and cancer research for years. Saccharomyces cerevisiae contains two paralogs of TOR, Tor1 and Tor2, which exist in their respective multi-subunit complexes TORC1 and TORC2. TORC2 has been found to regulate cell polarity, endocytosis, and actin polymerization in response to external stimuli, and studies have shown that the localization of TORC2 to the plasma membrane is essential for the complex's function. However, the upstream regulatory mechanisms of TORC2 still remain largely unknown. Ras proteins are of interest because they contain a C-terminal motif that targets the GTPase to the membrane, and relationships between homologs of TOR and Ras-GTPases have been found in other model organisms. Through this project, my main aim is to understand more about the potential relationship between TORC2 and Ras-GTPases of Saccharomyces cerevisiae by analyzing the role of Ras proteins in the complex’s localization. 

I would like to extend my deepest gratitude toward the Pergo Fund for giving me the opportunity to engage in such an immersive and life-changing experience this summer. Over the course of the 8+ weeks, I have not only gathered and improved on many technical skills within the lab, but I have also learned how to be more patient and understanding of the challenges that come with research. More importantly, I feel like I have made significant progress in science communication through this program, which has opened my eyes to how important effective delivery is. Furthermore, this program has given me such a strong support network in my mentor, advisors, and peers, and coming out of it, I feel less alone in pursuing even the hardest of endeavors.