ArticlePloS one2017
IRSp53 accumulates at the postsynaptic density under excitatory conditions.
Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 34 citations in OpenAlex.
- Two-dimensional molecular condensation in cell signaling and mechanosensing.Acta biochimica et biophysica Sinica · 2023Review
- Modification of the synaptic cleft under excitatory conditions.Frontiers in synaptic neuroscience · 2023Article
- IRSp53 promotes postsynaptic density formation and actin filament bundling.The Journal of cell biology · 2022Article
- Optimization of protocols for pre-embedding immunogold electron microscopy of neurons in cell cultures and brains.Molecular brain · 2021Article
- Revisiting I-BAR Proteins at Central Synapses.Frontiers in neural circuits · 2021Review
- Activity-dependent redistribution of CaMKII in the postsynaptic compartment of hippocampal neurons.Molecular brain · 2020Article
- Stimulation induces gradual increases in the thickness and curvature of postsynaptic density of hippocampal CA1 neurons in slice cultures.Molecular brain · 2019Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
IRSp53 (BAIAP2) is an abundant protein at the postsynaptic density (PSD) that binds to major PSD scaffolds, PSD-95 and Shanks, as well as to F-actin. The distribution of IRSp53 at the PSD in cultured hippocampal neurons was examined under basal and excitatory conditions by immuno-electron microscopy. Under basal conditions, label for IRSp53 is concentrated at the PSD. Upon depolarization by application of a medium containing 90 mM K+, the intensity of IRSp53 label at the PSD increased by 36±7%. Application of NMDA (50 μM) yielded 53±1% increase in the intensity of IRSp53 label at the PSD compared to controls treated with APV, an NMDA antagonist. The accumulation of IRSp53 label upon application of high K+ or NMDA was prominent at the deeper region of the PSD (the PSD pallium, lying 40-120 nm from the postsynaptic plasma membrane). IRSp53 molecules that accumulate at the distal region of the PSD pallium under excitatory conditions are too far from the plasma membrane to fulfill the generally recognized role of the protein as an effector of membrane-bound small GTPases. Instead, these IRSp53 molecules may have a structural role organizing the Shank scaffold and/or linking the PSD to the actin cytoskeleton.
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