Sarah Kowalczyk, Aline Winkelmann, Birthe Smolinsky, Benjamin Förstera, Ines Neundorf, Guenter Schwarz and Jochen C. Meier Direct binding of GABAA receptor β2 and β3 subunits to gephyrin European Journal of Neuroscience 37
GABAA receptor (GABAAR) α-subunits were recently shown to interact with gephyrin, which contributes to postsynaptic receptor stabilisation. We show that the C-terminal parts of cytoplasmic loops between transmembrane domains 3 and 4 of GABAAR β2 and β3 subunits also interact with gephyrin. Compared with the GlyR β loop, the binding of GABAAR β2 and β3 loops to gephyrin showed a twenty fold lower affinity, which is in the range of the KD values that were determined for GABAAR α-subunits. The identified gephyrin-binding sequences of β2 and β3 subunits also mediate postsynaptic localisation of corresponding GlyR α1-GABAAR β chimaeras in cortical neurons. Thus, at least five different GABAAR subunits can interact with gephyrin.
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