Grogan, LenaMcClean, NathanielShapiro, Paul, Ph.D.2023-10-172023-10-172023-10-13http://hdl.handle.net/10713/20948Fall Grad Gathering, October 13, 2023The role of extracellular signal-regulated kinase 1/2 (ERK1/2) in signaling pathways in cells is crucial for cell proliferation. Within specific types of cancers, a member of this pathway, BRAF, is mutated at the valine (V)600 position so that this pathway is continuously activated, leading to uncontrolled proliferation. A docking site in ERK1/2 is of interest for inhibitors to control activation of downstream proteins responsible for transcription.1 A compound has been developed to target a substrate docking site and was found to target a specific cysteine2. This residue has been mutated via CRISPR CAS9 in both ERK1 and ERK2 and the proposed studies investigate the effects the ERK1/2 cysteine mutations have on A375 cell melanoma cells regarding cell signaling and proliferation.en-USAttribution-NonCommercial-NoDerivatives 4.0 Internationalhttp://creativecommons.org/licenses/by-nc-nd/4.0/CysteineMAP Kinase Signaling SystemMelanomaCell ProliferationProto-Oncogene Proteins B-rafThe role of a cysteine residue within an ERK1/2 substrate docking site on signaling and proliferation of melanoma cells containing BRAF mutationsPoster/Presentation