TY - JOUR T1 - International Union of Pharmacology. LXX. Subtypes of γ-Aminobutyric Acid<sub>A</sub> Receptors: Classification on the Basis of Subunit Composition, Pharmacology, and Function. Update JF - Pharmacological Reviews JO - Pharmacol Rev SP - 243 LP - 260 DO - 10.1124/pr.108.00505 VL - 60 IS - 3 AU - Richard W. Olsen AU - Werner Sieghart Y1 - 2008/09/01 UR - http://pharmrev.aspetjournals.org/content/60/3/243.abstract N2 - In this review we attempt to summarize experimental evidence on the existence of defined native GABAA receptor subtypes and to produce a list of receptors that actually seem to exist according to current knowledge. This will serve to update the most recent classification of GABAA receptors (Pharmacol Rev 50:291–313, 1998) approved by the Nomenclature Committee of the International Union of Pharmacology. GABAA receptors are chloride channels that mediate the major form of fast inhibitory neurotransmission in the central nervous system. They are members of the Cys-loop pentameric ligand-gated ion channel (LGIC) superfamily and share struc-tural and functional homology with other members of that family. GABAA receptors are assembled from a family of 19 homologous subunit gene products and form numerous, mostly hetero-oligomeric, pentamers. Such receptor subtypes with properties that depend on subunit composition vary in topography and ontogeny, in cellular and subcellular localization, in their role in brain circuits and behaviors, in their mechanisms of regulation, and in their pharmacology. We propose several criteria, which can be applied to all the members of the LGIC superfamily, for including a receptor subtype on a list of native hetero-oligomeric subtypes. With these criteria, we develop a working GABAA receptor list, which currently includes 26 members, but will undoubtedly be modified and grow as information expands. The list is divided into three categories of native receptor subtypes: “identified,” “existence with high probability,” and “tentative.” ER -