| Literature DB >> 29429936 |
Lucas Matt1, Karam Kim1, Anne C Hergarden1, Tommaso Patriarchi1, Zulfiqar A Malik2, Deborah K Park1, Dhrubajyoti Chowdhury1, Olivia R Buonarati1, Peter B Henderson1, Çiğdem Gökçek Saraç3, Yonghong Zhang4, Durga Mohapatra5, Mary C Horne2, James B Ames4, Johannes W Hell6.
Abstract
Despite the central role PSD-95 plays in anchoring postsynaptic AMPARs, how PSD-95 itself is tethered to postsynaptic sites is not well understood. Here we show that the F-actin binding protein α-actinin binds to the very N terminus of PSD-95. Knockdown (KD) of α-actinin phenocopies KD of PSD-95. Mutating lysine at position 10 or lysine at position 11 of PSD-95 to glutamate, or glutamate at position 53 or glutamate and aspartate at positions 213 and 217 of α-actinin, respectively, to lysine impairs, in parallel, PSD-95 binding to α-actinin and postsynaptic localization of PSD-95 and AMPARs. These experiments identify α-actinin as a critical PSD-95 anchor tethering the AMPAR-PSD-95 complex to postsynaptic sites.Entities:
Keywords: AMPA receptors; PSD-95; dendritic spines; hippocampus; synapse; α-actinin
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Year: 2018 PMID： 29429936 PMCID： PMC5963734 DOI： 10.1016/j.neuron.2018.01.036
Source DB: PubMed Journal: Neuron ISSN： 0896-6273 Impact factor: 17.173