A1: Molecular basis of glycine- and GABAA receptor clustering and signaling - A2: Inhibitory synapses and synaptic plasticity: structural and functional coupling of local synthesis with inhibitory ion channels

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Many postsynaptic membrane specializations harboring glycine- (GlyR) or -amino butyric acid (GABA) receptors also contain scaffolds of the peripheral membrane protein gephyrin. Whereas the contribution of gephyrin, which interacts with the GlyR  subunit, to the formation and maintenance of glycinergic synapses has been amply documented, the functional role of other GlyR associated proteins is still unclear. We have identified a set of proteins interacting with GlyR 2 subunits, which are possibly involved in regulating protein synthesis and/or actin dynamics. We would like to continue our research on the functional characterization of these GlyR interacting proteins using biochemical and molecular biological approaches. The contribution of the newly identified components of inhibitory synapses shall be analysed both on the morphological and functional level. It is conceivable that dynamic changes in the composition of the protein machinery underneath inhibitory synapses may contribute to activity-dependent plastic changes and functional adaptations of synapses. Moreover, these subsynaptic proteins could be involved in the formation and maintenance of inhibitory synapses, the regulation of their developmental changes or modifications and secondary signaling cascades.