Heterotrimeric G proteins are a protein family capable of causing many effects throughout the cell through the sheer enormity of signaling pathways they influence. Gα12 has been studied for its role in cell growth, apoptosis, adhesion, and migration. It has been shown to interact with protein phosphatase 5 (PP5) in biological pathways causing PP5 translocation, dephosphorylation of K+ channels, dephosphorylation of intestinal cell kinase, and the ASK1 pathway. Despite this knowledge, the specific location of binding between Gα12 and PP5 is unknown. In this experiment, I created an assay capable of determining the interaction between the TPR region of PP5 and Gα12. Using this assay, the activation states required for binding were determined. I also utilized a comprehensive Gα12 NAAIRS mutant library to determine the exact location necessary for binding between Gα12 and PP5.
