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Collybistin is a protein identified as a regulator of the localization of gephyrin, inducing the formation of submembrane gephyrin aggregates that accumulate glycine and GABA receptors. In 2000 it was identified as a gephyrin binding partner, and an important determinant of inhibitory postsynaptic membrane formation and plasticity.[1] Gephyrin and collybistin are recruited to developing postsynaptic membranes of inhibitory synapses by the trans-synaptic adhesion molecule neuroligin-2,[2] where they provide the scaffold for the clustering of inhibitory postsynaptic receptors to form a functioning inhibitory synapse.


  1. ^ Betz, Heinrich; Kins, Stefan; Kirsch, Joachim (2000). "Collybistin, a newly identified brain-specific GEF, induces submembrane clustering of gephyrin". Nature Neuroscience. 3 (1): 22–9. doi:10.1038/71096. PMID 10607391. 
  2. ^ Poulopoulos, Alexandros; Aramuni, Gayane; Meyer, Guido; Soykan, Tolga; Hoon, Mrinalini; Papadopoulos, Theofilos; Zhang, Mingyue; Paarmann, Ingo; et al. (2009). "Neuroligin 2 Drives Postsynaptic Assembly at Perisomatic Inhibitory Synapses through Gephyrin and Collybistin". Neuron. 63 (5): 628–42. doi:10.1016/j.neuron.2009.08.023. PMID 19755106.