We aim to advance quantitative proteomics technology and combine these methods with computational, biochemical, and imaging approaches to study the structure of the cytoplasm, nucleocytoplasmic partitioning, and the control of protein expression levels.

Outlined below are a few examples of questions and research goals we are interested in. 

  • Developing multiplexed MS methods for quantifying low abundant proteins (~1 nM) such as transcription factors and kinases
  • Make quantitative multiplexed proteomics compatible with cost-effective mass spectrometers. 
  • How are protein abundances controlled? How much do transcription, translation, and degradation contribute to adapting protein abundances in different growth conditions?
  • Can we add prokaryotic proteomes (several thousand proteins that have never seen a nucleus) to eukaryotic systems and measure their nuclear partitioning to determine which physiochemical properties of proteins determine flux across the nuclear membrane? 
  • Can we systematically measure the binding constants for active transport of proteins into and out of the nucleus via importins and exportins for the entire proteome? Can we integrate these measurements with other data to predict nucleocytoplasmic partitioning?
  •  Can we develop methods to measure the strength of protein-protein interactions and better understand the nature of cytoplasm?