Postsynaptic density (PSD)-95-like membrane-associated guanylate kinases (PSD-MAGUKs) are scaffold proteins in PSDs that cluster signaling molecules near NMDA receptors. PSD-MAGUKs share a common domain structure, including three PDZ (PDZ1/2/3) domains in their N-terminus. While multiple domains enable the PSD-MAGUKs to bind various ligands, the contribution of each PDZ domain to synaptic organization and function is not fully understood. Here, we focused on the PDZ1/2 domains of PSD-95 that bind NMDA-type receptors, and studied the specific roles of the ligand binding of these domains in the assembly of PSD proteins, synaptic properties of hippocampal neurons, and behavior, using ligand binding-deficient PSD-95 cDNA knockin (KI) mice.
Pubmed ID: 23268962 RIS Download
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Mus musculus with name C57BL/6J from IMSR.
View all literature mentionslaboratory mouse with name BALB/cAnNCrl from MGI.
View all literature mentionsThis monoclonal targets TARPGamma2/4/8
View all literature mentionsThis monoclonal targets PSD-95 MAGUK scaffolding protein
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