Biochemical and Biophysical Research CommunicationsNeurosciencePeer-reviewed journal article
FRMPD2: a novel GluN2A-interacting scaffold protein in synaptic excitatory transmission
Abstract
The scaffold proteins FRMPD2 is localized at the basolateral membranes of polarized epithelial cells and associated with tight junction formation. But the expression and function of FRMPD2 in vivo remain unknown. Here, we found that postsynaptic FRMPD2 effectively alters the neuronal excitability by regulating NMDARs-component excitatory synaptic transmission in adult hippocampus. FRMPD2 anchors the NMDAR subunit GluN2A at the synapses without changing the total NMDAR expression. By using of Co-IP, Pull Down and SPR, the second PDZ (PDZ2) domain of FRMPD2 direct and binds to the C-terminus of GluN2A. Our study discover that a novel scaffold protein FRMPD2 regulates synaptic excitatory in a PDZ2 domain-dependent manner in adult hippocampus.
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