Inhibitory neurotransmission is primarily mediated by γ-aminobutyric acid (GABA) activating synaptic GABA type A receptors (GABA A R). In schizophrenia, presynaptic GABAergic signaling deficits are among the most replicated findings; however, postsynaptic GABAergic deficits are less well characterized. Our lab has previously demonstrated that although there is no difference in total protein expression of the α1-6, β1-3 or γ2 GABA A R subunits in the superior temporal gyrus (STG) in schizophrenia, the α1, β1 and β2 GABA A R subunits are abnormally N-glycosylated. N-glycosylation is a posttranslational modification that has important functional roles in protein folding, multimer assembly and forward trafficking. To investigate the impact that altered N-glycosylation has on the assembly and trafficking of GABA A Rs in schizophrenia, this study used western blot analysis to measure the expression of α1, α2, β1, β2 and γ2 GABA A R subunits in subcellular fractions enriched for endoplasmic reticulum (ER) and synapses (SYN) from STG of schizophrenia (N=16) and comparison (N=14) subjects and found evidence of abnormal localization of the β1 and β2 GABA A R subunits and subunit isoforms in schizophrenia. The β2 subunit is expressed as three isoforms at 52 kDa (β2 52 kDa), 50 kDa (β2 50 kDa) and 48 kDa (β2 48 kDa). In the ER, we found increased total β2 GABA A R subunit (β2 ALL) expression driven by increased β2 50 kDa, a decreased ratio of β2 48 kDa:β2 ALL and an increased ratio of β2 50 kDa:β2 48 kDa. Decreased ratios of β1:β2 ALL and β1:β2 50 kDa in both the ER and SYN fractions and an increased ratio of β2 52 kDa:β2 48 kDa at the synapse were also identified in schizophrenia. Taken together, these findings provide evidence that alterations of N-glycosylation may contribute to GABAergic signaling deficits in schizophrenia by disrupting the assembly and trafficking of GABA A Rs.