Prof. Matthew Torres, Georgia Tech

Post-translational regulation of G proteins: Towards elucidating PTM codes in cell signaling

A growing body of evidence from studies with histone proteins, RNA polymerase II, p53, tubulin and others suggest that PTMs often function in concert to regulate biological function. At the level of a single protein, PTMs can alter protein function by manifesting changes in protein structure and conformation, recruitment of binding proteins or through direct effects on catalytic activity. Over the last few decades, increasingly sophisticated and robust methods of PTM detection and quantitation (e.g. mass spectrometry) have uncovered a plethora of different PTM types (> 300 known PTMs). A recurring theme is that PTMs regulate protein interaction landscapes – the array of potential protein-protein interactions that can exist for a protein. Emerging evidence has revealed dynamic and complex PTM regulation of heterotrimeric G proteins, which are signaling complexes essential for transduction of extracellular signals into intracellular responses and therefore critical for the survival of multi-cellular organisms. We now have an extensive understanding of the structures and biophysical mechanisms underlying G protein signal transduction. However, our understanding of how dynamic PTMs coordinate signal transduction is underwhelming. Not unlike the combinatorial codes that regulate chromatin and tubulin, we are interested in elucidating how PTMs coordinate signal transduction, effector association and pleiotropic downstream signal responses.

For more information contact Prof. Wendy Kelly (404-385-1154).