ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2011
PSD-95 is required to sustain the molecular organization of the postsynaptic density.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 174 papers.
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Who cites it
174 citing papers in PubMed, 304 citations in OpenAlex.
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- Phase separation instead of binding strength determines target specificities of MAGUKs.Nature chemical biology · 2026Article
- Altered synaptic and astrocytic proteins in Lewy body disorders associated withBrain communications · 2026Article
- Calcium signaling and postsynaptic density dynamics: the roles of calmodulin in synaptic protein regulation.Frontiers in molecular neuroscience · 2026Review
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- High-Pressure Freezing EM Tomography of Entire Ribbon Synapses in the Retina.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2025Article
- Revealing acute consequences of rapid degradation of synaptic fusion proteins at individual synapses using Auxin-Inducible Degron 2 technology.Communications biology · 2025Article
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114 more citing papers are in PubMed but not listed here.
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Authors and funding
10 authors at 4 institutions in 2 countries.
Funding
Abstract
PSD-95, a membrane-associated guanylate kinase, is the major scaffolding protein in the excitatory postsynaptic density (PSD) and a potent regulator of synaptic strength. Here we show that PSD-95 is in an extended configuration and positioned into regular arrays of vertical filaments that contact both glutamate receptors and orthogonal horizontal elements layered deep inside the PSD in rat hippocampal spine synapses. RNA interference knockdown of PSD-95 leads to loss of entire patches of PSD material, and electron microscopy tomography shows that the patchy loss correlates with loss of PSD-95-containing vertical filaments, horizontal elements associated with the vertical filaments, and putative AMPA receptor-type, but not NMDA receptor-type, structures. These observations show that the orthogonal molecular scaffold constructed from PSD-95-containing vertical filaments and their associated horizontal elements is essential for sustaining the three-dimensional molecular organization of the PSD. Our findings provide a structural basis for understanding the functional role of PSD-95 at the PSD.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.