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Published on: August 2, 2019
Regulation of AMPA receptor trafficking by delta-catenin
Tomoyo Ochiishi1, Kensuke Futai, Kenichi Okamoto
1Neuroscience Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), 1-1-1 Higashi, Tsukuba, Ibaraki 305-8566, Japan. tomoyo.ochiishi@aist.go.jp
Abstract:
delta-catenin is a protein that binds to the classical cadherins and to synaptic scaffolding proteins in a manner which allows the protein to serve as a link between the adherens junction and the postsynaptic complex. Here we show the regulatory role of delta-catenin on synaptic transmission. delta-catenin increased the AMPA receptor-mediated EPSC, but had no significant effect on the NMDA receptor-mediated EPSC. The effect of delta-catenin on the AMPAR EPSC was mediated by its PDZ ligand. delta-catenin regulates the surface expression of GluR2 in the dendritic spines of neurons. Immunoprecipitation revealed that delta-catenin bound to GRIP-1. In COS7 cells, co-transfection of delta-catenin, GRIP and GluR2 showed that delta-catenin regulates the membrane localization of GRIP through its PDZ ligand and increased the surface expression of GluR2. This study directly shows that delta-catenin is essential for the trafficking and positioning GluR2 in the spine and thus further links delta-catenin to neuronal plasticity.
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