My research stems from our recent observation that proteins which interact in multi-protein partnerships or complexes are tightly co-expressed, with the steady state abundance of each member protein set at the abundance of the lowest expressed protein constituent. This post-transcriptional mechanism, which we term "Stoichiometric Buffering" likely stems from increased stability conferred by protein-protein interactions. My project seeks to elucidate the molecular details underlying this post-translational regulatory mechanism. Previous work by the Munger lab and collaborating labs has gathered expression and protein quantitative trait loci (eQTL & pQTL, respectively) data from Diversity Outbred (DO) mouse liver and kidney. Using these data, we predicted for stoichiometrically buffered protein complexes by screening for proteins whose abundance does not correlate to their own mRNA expression, but rather to the abundance of another protein. Currently, I am validating one pair of candidates (NNT and TMEM68), developing a pipeline for further validations, and using polysome profiling of DO founder strain livers to improve our predictions by introducing a measure of translation on top of steady state protein levels.
BS, Cell Biology. University of California - Davis, Davis, CA
MS, Biology, California State University - Chico, Chico, CA