We are interested in understanding how eukaryotic cells regulate their growth in response to both environmental stimuli as well as intracellular signals.  We have been particularly focused on the role of a conserved signaling network, defined by its central player the TOR kinase, so named because it is the target of the antibiotic and anti-tumor drug rapamycin.  TOR is a large (~280 kDa) protein that assembles with an overlapping yet distinct set of interacting proteins to form two different complexes, termed TOR Complex 1 and 2 (TORC1 and TORC2).   Together these complexes collaborate to control both temporal as well as spatial aspects of cell growth, including nutrient-regulated gene expression, ribosome biogenesis, membrane trafficking, and polarized cell growth. 

Our efforts have been directed toward answering several fundamental questions regarding these complexes, using primarily budding yeast as a model experimental system.  Some of these questions include: i) how do TORC1 and TORC2 assemble and where are they localized within cells? ii) what are the substrates for these complexes and how is TOR kinase activity regulated? iii) what is the scope of cellular processes controlled either uniquely or collaboratively by TORC1 versus TORC2?  Our goal is to understand how TOR signaling contributes to the function of normal cells and, ultimately, to understand its role in the progression of distinct diseases, including cancer.  

Please peruse our recent publications to determine the nature of our specific approaches and questions presently ongoing in the lab.