GABAA receptor trafficking is regulated by many protein kinases, including PKC, PKA, and fyn. However, to date, the role of these protein kinases has not yet been studied in the trafficking of GABAA receptors, especially following EtOH exposure. Chronic EtOH consumption decreases association of PKCγ with α1 GABAA receptors and increases association of PKCγ with α4 GABAA receptors, accompanied by a decreased expression of the α1 subunit and an increased expression of α4 at the cell surface in cerebral cortex (Kumar et al. 2002). However, there were no alterations in the association of PKCγ with GABAA receptors in the α1 subunit expression following chronic EtOH administration in the hippocampus (Kumar et al. 2004). The increased association of PKCγ with α4 GABAA receptors may phosphorylate GABAA receptor subunits and prevent recognition of the receptor by AP-2, thus preventing its internalization. Indeed, phosphorylation of GABAA receptor subunits reduced the binding of receptors with AP-2 and subsequent internalization (Kittler et al. 2008). Moreover, reduced PKC-dependent GABAA receptor phosphorylation increases receptor binding to the AP-2 and promotes receptor endocytosis (Terunuma et al. 2008). Chronic
