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000163742 0247_ $$2doi$$a10.1371/journal.pbio.3001503
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000163742 1001_ $$aSchmerl, Bettina$$b0
000163742 245__ $$aThe synaptic scaffold protein MPP2 interacts with GABAA receptors at the periphery of the postsynaptic density of glutamatergic synapses.
000163742 260__ $$aLawrence, KS$$bPLoS$$c2022
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000163742 520__ $$aRecent advances in imaging technology have highlighted that scaffold proteins and receptors are arranged in subsynaptic nanodomains. The synaptic membrane-associated guanylate kinase (MAGUK) scaffold protein membrane protein palmitoylated 2 (MPP2) is a component of α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptor-associated protein complexes and also binds to the synaptic cell adhesion molecule SynCAM 1. Using superresolution imaging, we show that-like SynCAM 1-MPP2 is situated at the periphery of the postsynaptic density (PSD). In order to explore MPP2-associated protein complexes, we used a quantitative comparative proteomics approach and identified multiple γ-aminobutyric acid (GABA)A receptor subunits among novel synaptic MPP2 interactors. In line with a scaffold function for MPP2 in the assembly and/or modulation of intact GABAA receptors, manipulating MPP2 expression had effects on inhibitory synaptic transmission. We further show that GABAA receptors are found together with MPP2 in a subset of dendritic spines and thus highlight MPP2 as a scaffold that serves as an adaptor molecule, linking peripheral synaptic elements critical for inhibitory regulation to central structures at the PSD of glutamatergic synapses.
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000163742 650_7 $$2NLM Chemicals$$aMembrane Proteins
000163742 650_7 $$2NLM Chemicals$$aReceptors, AMPA
000163742 650_7 $$2NLM Chemicals$$aReceptors, GABA-A
000163742 650_2 $$2MeSH$$aMembrane Proteins: metabolism
000163742 650_2 $$2MeSH$$aPost-Synaptic Density: metabolism
000163742 650_2 $$2MeSH$$aReceptors, AMPA: metabolism
000163742 650_2 $$2MeSH$$aReceptors, GABA-A
000163742 650_2 $$2MeSH$$aSynapses: metabolism
000163742 7001_ $$aGimber, Niclas$$b1
000163742 7001_ $$aKuropka, Benno$$b2
000163742 7001_ $$aStumpf, Alexander$$b3
000163742 7001_ $$aRentsch, Jakob$$b4
000163742 7001_ $$aKunde, Stella-Amrei$$b5
000163742 7001_ $$avon Sivers, Judith$$b6
000163742 7001_ $$aEwers, Helge$$b7
000163742 7001_ $$0P:(DE-2719)2810725$$aSchmitz, Dietmar$$b8$$udzne
000163742 7001_ $$aFreund, Christian$$b9
000163742 7001_ $$aSchmoranzer, Jan$$b10
000163742 7001_ $$0P:(DE-2719)2814334$$aRademacher, Nils$$b11$$udzne
000163742 7001_ $$00000-0003-4933-7846$$aShoichet, Sarah A$$b12
000163742 773__ $$0PERI:(DE-600)2126773-X$$a10.1371/journal.pbio.3001503$$gVol. 20, no. 3, p. e3001503 -$$n3$$pe3001503$$tPLoS biology$$v20$$x1544-9173$$y2022
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