Our laboratory develops mass spectrometry and computational techniques to understand the fundamental mechanisms underlying disease onset and progression. Our current research focuses on post-transcriptional regulation of proteins under development, aging, and cellular stress.
The proteome is sculpted by post-transcriptional forces. A significant portion of protein variance cannot be explained by transcript levels. This non-correlation is best observed in dynamical systems: while an abundant transcript generally produces a more abundant protein over a low-abundance transcript (high correlation across genes), transcript fold-changes upon stimuli poorly predict those of proteins (low correlation across samples) Some RNA-protein decoupling is traceable to physical constraints or buffering but a majority is due to the many layers of post-transcriptional and post-translational regulations that modify protein levels, including transcript splicing, stability, and translation rates (post-transcriptional) as well as protein localization, modifications, and degradation (post-translational). Because proteins are the primary effector molecules in biology, knowledge into the mechanisms that control protein levels carries fundamental significance to diverse areas of studies.
Proteins carry out the majority of biological functions. Cellular protein abundance is controlled by transcript level as well as post-transcriptional and post-translational mechanisms. Our lab is interested in how alternative splicing, mRNA stability, protein synthesis and degradation, as well as protein-protein interaction orchestrate a functional proteome. By unraveling how stressors disrupt these dynamic processes, we hope to apply the gained knowledge toward new strategies to remediate stress responses in aging and diseases.