Fig. 9 | Nature Communications

Fig. 9

From: A unique intracellular tyrosine in neuroligin-1 regulates AMPA receptor recruitment during synapse differentiation and potentiation

Fig. 9

Working model for the role of Nlg1 tyrosine phosphorylation in synapse differentiation and potentiation. Phosphorylated Nlg1 (mimicked by Nlg1-Y782A) preferentially recruits PSD-95 and AMPARs and favors dendritic spines. In contrast, non-phosphorylated Nlg1 (mimicked by Nlg1-Y782F) diffuses out of dendritic spines and interacts preferentially with gephyrin, thus preventing PSD-95 and AMPAR recruitment and resulting in silent synapses. NMDARs are recruited independently of mutations in the Nlg1 intracellular domain, consistent with a direct extracellular coupling to Nlg1. A fraction of Nlg1-Y782F associates with gephyrin scaffolds and GABAA receptors to make inhibitory synapses

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