Dr. Matthew Torres (Candidate for the Macromolecular Assemblies position)
Department of Biochemistry and Biophysics, University of North Carolina at Chapel Hill
Thursday, December 1, 2011 - 11:00 to 12:00
Room 1116-1118, Marcus Nanotechnology Bldg
Post-translational regulation of G proteins: Towards elucidating combinatorial codes in cell signaling
Now well into the era of genomics and proteomics, it is widely appreciated that understanding the function of individual genes or proteins, although necessary, is often not sufficient to explain the complex behavior observed in living organisms. Indeed, placing context on the dynamic network of relationships that exist between multiple proteins is now one of the greatest challenges in Biology. Post-translational modifications (PTMs), which can be readily quantified by mass spectrometry (MS), often mediate these dynamic relationships through enhancement or disruption of protein interactions or catalytic properties that can result in changes in specificity, stability, or cellular localization. G proteins – essential signal mediators in all multi-cellular organisms – are well positioned to serve as targets of post-translational regulation. I will present emerging evidence that G proteins (including Ga and Gbg subunits) are regulated by PTMs such as phosphorylation and ubiquitination. Moreover, I will discuss how modifying enzymes recently discovered for the Ga subunit have uncovered new potential modes of regulating signal transduction in a spatiotemporal context. Finally, I will discuss future efforts to understand how PTMs are coordinated to regulate this and other signal transduction pathway components.