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.
Lab Website
https://maggielamlab.org
Publications
paper.maggielamlab.org
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.