GABA transporter 3 (GAT3) is mainly located in the astrocytes in the brain, and it’s responsible for regulating brain inhibitory neurotransmission through the reuptake of GABA molecules from the synapse. Alterations in GAT3 levels are related to multiple neurodegenerative and neurological diseases making it a promising therapeutic target. My research aims to analyze wild-type and C-terminal truncated GAT3 using computational and molecular biology tools to understand the effect of the C-terminal region on the protein’s dynamic, localization, and trafficking. Due to the GAT3 structure being unknown homology modeling using Discover Studios 2016 was done to predict the outward (oGAT3) and inward (iGAT3) open confirmations for both the wild-type (GAT3+C) and the mutant (GAT3-C) structures. 100ns molecular dynamics (MD) was performed for an initial check of the structural stability, following that substrates docking was performed using AutoDock 1.5.7 to the outward open conformation resulting from MD for both targeted structures. The 100ns MD simulations show promising results of a possible impact of the C-terminal on GAT3 structural stability especially the inward open confirmation as the analysis suggests the C-terminal pushing a stronger closure of the extracellular gate and a bigger opening of the intracellular gate, but to fully understand the impact of the mutation a longer 1000ns simulation will be performed to the inward, outward, and docked outward conformations representing the wild-type and mutant GAT3. Cells will be transfected with pcDNA3.1(+) vector containing HA-tagged wild-type or mutant GAT3 and the localization and trafficking pattern of GAT3 will be analyzed.