Glenn Dillon2019-08-222019-08-221998-05-012014-01-14https://hdl.handle.net/20.500.12503/29336Mingjun, Fang. Modulation of GABAA Receptor Function by Tyrosine Phosphorylation. Master of Science (Biomedical Sciences), May, 1998, 32 pp., 6 illustrations, bibliography, 42 titles. The goal of this study was to determine the modulation of GABAA receptor function by tyrosine kinase phosphorylation, and to detect which subunit is phosphorylated to alter the GABA-induced chloride currents. From previous studies, we suggested that protein tyrosine phosphorylation may maintain GABAA receptor function. Here we tested the hypothesis that tyrosine phosphorylation modulates other GABAA receptor subtypes e.g., α1β2γ2 and α6β2γ2, and subsequently attempted to determine which subunit(s) may be phosphorylated. Our results support the hypothesis that PTK phosphorylation may maintain GABAA receptor function. In addition, we suggest this tyrosine phosphorylation occurs at the γ2 subunit of the receptor.application/pdfenCellular and Molecular PhysiologyChemical Actions and UsesChemicals and DrugsLife SciencesMedicine and Health SciencesNervous SystemNeuroscience and NeurobiologyOther Neuroscience and NeurobiologyOther PhysiologyPhysiologyTissuesModulationGABAA receptor functiontyrosine kinase phosphorylationchloride currentsγ2 subunitThesis