The Torres lab has been awarded a four year, $1.2 million grant by the National Institutes of General Medical Sciences to investigate a newly discovered regulatory mechanism that controls G protein signaling, a process essential for the transduction of extracellular signals (such as hormones, neurotransmitters, and photons of light), and the target of most pharmaceutical drugs.
Spawned by their development and application of a custom bioinformatics software tool (called SAPH-ire) 1, the Torres lab discovered a new way in which G protein signaling is regulated by phosphorylation – an enzyme-driven chemical modification of specific amino acid side chains found in most proteins. The newly discovered phospho-regulatory element, like G proteins themselves, is well conserved throughout eukaryotes, which will enable Torres and his lab to investigate how the element functions across diverse organisms such as budding yeast and humans. The National Institutes of Health grant will also provide funding to determine the biochemical mechanism of G protein phosphorylation – including the enzymes that activate the regulatory element in coordination with other cellular processes including cell division and stress. Through these and other approaches, Torres hopes to determine whether his lab has discovered a protein mechanism that is not only fundamental to the process of G protein signaling in all eukaryotes, but also a possible alternative target for pharmaceutical drug therapies.
Dewhurst, H. M., Choudhury, S. & Torres, M. P. Structural Analysis of PTM Hotspots (SAPH-ire)--A Quantitative Informatics Method Enabling the Discovery of Novel Regulatory Elements in Protein Families. Mol. Cell. Proteomics 14, 2285–97 (2015).