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Synaptic localization of membrane‐associated guanylate kinase‐interacting protein mediated by the pleckstrin homology domain

Membrane‐associated guanylate kinase‐interacting protein (MAGUIN) has been identified as a protein binding postsynaptic density (PSD)‐95 and synaptic scaffolding molecule (S‐SCAM). MAGUIN has one sterile α motif, one conserved region in connector enhancer of ksr (Cnk) (CRIC), one PSD‐95/Dlg‐A/ZO‐1 (PDZ) and one pleckstrin homology (PH) domain. There are two isoforms, MAGUIN‐1 and ‐2. MAGUIN‐1 binds the PDZ domains of PSD‐95 and S‐SCAM by the C‐terminus, whereas MAGUIN‐2 does not bind to PSD‐95 or S‐SCAM. Here, we have determined that MAGUIN‐2 is also localized at synapses and that the synaptic localization of MAGUIN depends on the pleckstrin homology domain. The overexpressed C‐terminal PDZ‐binding region inhibits the synaptic targeting of PSD‐95. Furthermore, the synaptic targeting of MAGUIN does not require N‐methyl‐d‐aspartate (NMDA) receptor activity. These findings suggest that MAGUIN‐1 and ‐2 are recruited to synapses by the PH domain and that MAGUIN‐1 subsequently interacts with PSD‐95 at synapses.