The G12/13 subfamily of G protein α subunits provide conduits between cell-surface receptors and an expansive array of target proteins that are important in a wide range of biological events. My research project specifically focused on studying the interaction between Gα12 and its target protein ARAF. Activation of the protein ARAF by Gα12 upregulates RFFL E3 ubiquitin ligase, which leads to destabilization of PRR5L, a subunit of mammalian target of rapamycin complex 2 (mTORC2). This signaling pathway is crucial for fibroblast migration and pulmonary fibrosis development. My research project was to identify structural features that are critical in the interaction between Gα12 and ARAF. I conducted pulldown experiments with various Gα12 cassette substitution mutants, in which regions of six amino acids in Gα12 were replaced by the filler sequence Asn-Ala-Ala-Ile-Arg-Ser (NAAIRS). Preliminary results indicate a significant disruption in Gα12 ability to interact with ARAF with NAAIRS substitution near the N-terminus region.