In the central nervous system inhibitory neurotransmission is primarily achieved through activation of receptors for gamma-aminobutyric acid (GABA). Three types of GABA receptors have been identified on the basis of their pharmacology and electrophysiology. The predominant type, termed GABAA and a recently identified type, GABAC, have integral chloride channels, whereas GABAB receptors couple to separate K+ or Ca2+ channels via G-proteins. By analogy to nicotinic acetylcholine receptors, native GABAA receptors are believed to be heterooligomers of five subunits, drawn from five classes (alpha, beta, gamma, delta, epsilon/chi). An additional class, called rho, is often categorized with GABAA receptor subunits due to a high degree of sequence similarity. However, rho subunits are capable of forming functional homooligomeric and heterooligomeric receptors, whereas GABAA receptors only express efficiently as heterooligomers. Intriguingly, the pharmacological properties of receptors formed from rho subunits are very similar to those exhibited by GABAC receptors and rho subunits and GABAC responses have been colocalized to the same retina cells, indicating that rho subunits are the sole components of GABAC receptors. In contrast, the propensity of GABAA receptor and rho subunits to form multimeric structures and their coexistence in retinal cells suggests that GABAC receptors might be heterooligomers of rho and GABAA receptor subunits. This review will summarize our current understanding of the molecular composition of GABAC receptors based upon studies of rho subunit assembly.