The Postsynaptic Architecture of Excitatory Synapses: A More Quantitative View

Sheng, Morgan; Hoogenraad, Casper C.

doi:10.1146/annurev.biochem.76.060805.160029

Cited by 1,003Neuroscience and Neuropharmacology ResearchGenetics and Neurodevelopmental DisordersReceptor Mechanisms and Signaling

The Postsynaptic Architecture of Excitatory Synapses: A More Quantitative View

Sheng, Morgan, Hoogenraad, Casper C.·2007·Annual Review of Biochemistry

DOI 10.1146/annurev.biochem.76.060805.160029

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Abstract

Excitatory (glutamatergic) synapses in the mammalian brain are usually situated on dendritic spines, a postsynaptic microcompartment that also harbors organelles involved in protein synthesis, membrane trafficking, and calcium metabolism. The postsynaptic membrane contains a high concentration of glutamate receptors, associated signaling proteins, and cytoskeletal elements, all assembled by a variety of scaffold proteins into an organized structure called the postsynaptic density (PSD). A complex machine made of hundreds of distinct proteins, the PSD dynamically changes its structure and composition during development and in response to synaptic activity. The molecular size of the PSD and the stoichiometry of many major constituents have been recently measured. The structures of some intact PSD proteins, as well as the spatial arrangement of several proteins within the PSD, have been determined at low resolution by electron microscopy. On the basis of such studies, a more quantitative and geometrically realistic view of PSD architecture is emerging.

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Crossref · 10.1146/annurev.biochem.76.060805.160029

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CaMKII is present in the brain at extraordinarily high levels, rivaling the levels of cytoskeletal proteins.
“Second, it is present in the brain at extraordinarily high levels, rivaling the levels of cytoskeletal proteins (63–67), suggesting that CaMKII may play a structural role (27, 68).”
From Synaptic memory and CaMKII (2023) · cites this paper as [66]
Given roughly 20-30 NMDARs in the PSD and ∼100 holoenzymes (∼1,200 CaMKII subunits), after NMDAR activation only a small fraction of subunits per holoenzyme would be directly bound to GluN2B.
“since there are roughly 20–30 NMDARs in the PSD (66, 143) and ∼100 holoenzymes [∼1,200 CaMKII subunits (65)], after NMDAR activation only a small fraction of subunits per holoenzyme would be directly bound to GluN2B.”
From Synaptic memory and CaMKII (2023) · cites this paper as [66]
Actin is largely excluded from the core of the PSD, interacting with proteins such as Shank and SAPAP in the pallium.
“However, actin is largely excluded from the core of the PSD, interacting with such proteins as Shank and SAPAP located in the deeper, cytoplasmic-facing layer of the PSD referred to as the pallium (66, 162, 322).”
From Synaptic memory and CaMKII (2023) · cites this paper as [66]
Although it is well established that CaMKII phosphorylates numerous synaptic proteins, an essential role for CaMKII phosphorylation of many of these targets largely remains elusive.
“It should be pointed out that, although it is well established that CaMKII phosphorylates numerous synaptic proteins (66, 434–437), as reviewed here, despite intensive research an essential role for CaMKII phosphorylation of many of these targets largely remains elusive.”
From Synaptic memory and CaMKII (2023) · cites this paper as [66]
Actin is largely excluded from the core of the PSD, and evidence suggests that, at least for the first hour, the changes in spine size are not accompanied by changes in the size of the PSD.
“Actin is largely excluded from the core of the PSD (66, 322), and evidence suggests that, at least for the first hour, the changes in spine size are not accompanied by changes in the size of the PSD (56).”
From Synaptic memory and CaMKII (2023) · cites this paper as [66]

The geometry of the spine neck determines the rate of calcium efflux into the dendrite shaft and hence the degree of elevation of calcium concentrations within the spine head, following NMDAR activation.
“The geometry of the spine neck determines the rate of calcium efflux into the dendrite shaft and hence the degree of elevation of calcium concentrations within the spine head, following n-methyl-D-aspartate receptor (NMDAR) activation (Bloodgood and Sabatini, 2005; Alvarez and Sabatini, 2007; Sheng and Hoogenraad, 2007).”
From Human Brain/Cloud Interface (2019) · cites this paper as Sheng and Hoogenraad, 2007
Recent evidence points toward the rapid exchange of PSD proteins, such as AMPARS and PSD-95, even between neighboring synapses under steady-state conditions.
“Remarkably, recent evidence points toward the rapid exchange of PSD proteins, such as AMPARS and PSD-95, even between neighboring synapses under steady-state conditions (Sheng and Hoogenraad, 2007).”
From Human Brain/Cloud Interface (2019) · cites this paper as Sheng and Hoogenraad, 2007
Longer-term changes in the PSD structure and composition (from hours to days) involve altered protein synthesis, either within the neuronal cell body, or dendrites.
“Longer-term changes in the PSD structure and composition (from hours to days) involve altered protein synthesis, either within the neuronal cell body, or dendrites (Sheng and Hoogenraad, 2007).”
From Human Brain/Cloud Interface (2019) · cites this paper as Sheng and Hoogenraad, 2007
The PSD dynamically regulates its components through protein phosphorylation, palmitoylation, local protein translation, the ubiquitin-proteasome system for protein degradation, and redistribution of specific proteins (e.g., CaMKIIα, AMPARs) both entering and leaving the PSD.
“The PSD dynamically regulates its components through protein phosphorylation, palmitoylation, local protein translation, the ubiquitin-proteasome system for protein degradation, and redistribution of specific proteins (e.g., CaMKIIα, AMPARs) both entering and leaving the PSD (Kim and Ko, 2006; Sheng and Hoogenraad, 2007).”
From Human Brain/Cloud Interface (2019) · cites this paper as Sheng and Hoogenraad, 2007
The activity-dependent modification of PSD proteins occurring over timescales of seconds to hours is believed to underlie plasticity processes such as LTP and LTD.
“For instance, the activity-dependent modification of PSD proteins occurring over timescales of seconds to hours is believed to underlie plasticity processes such as LTP and LTD (Sheng and Hoogenraad, 2007).”
From Human Brain/Cloud Interface (2019) · cites this paper as Sheng and Hoogenraad, 2007

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Identification of activity‐regulated proteins in the postsynaptic density fraction
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Authors: Sheng, M., & Hoogenraad, C. C.
Affiliations: Howard Hughes Medical Institute (US)
Erasmus MC (NL)
ORCID: Sheng, Morgan
Hoogenraad, Casper C.
Venue: Annual Review of Biochemistry
Publisher: Annual Reviews
Published: 2007-06-07
Volume: 76
Issue: 1
Pages: 823-847
ISSN: 0066-4154 (ISSN-L)
1545-4509
DOI: 10.1146/annurev.biochem.76.060805.160029
OpenAlex: W2071318481
Cited by: 1,003
References: 154
Citations by year: 2026: 27 · 2025: 37 · 2024: 32 · 2023: 42 · 2022: 41 · 2021: 51 · 2020: 64 · 2019: 58 · 2018: 52 · 2017: 39 · 2016: 58 · 2015: 42 · 2014: 62 · 2013: 68 · 2012: 65
FWCI: 5.26
Type: journal article
Language: en
Open access: closed
Locations: Annual Review of Biochemistry (publishedVersion)
PubMed (publishedVersion)
EUR Research Repository (Erasmus University Rotterdam) (submittedVersion)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetics and Neurodevelopmental Disorders
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
Keywords: postsynaptic density, excitatory synapses, glutamatergic synapses, dendritic spines, synaptic structure, glutamate receptors, synaptic scaffolds, protein stoichiometry, postsynaptic membrane, synaptic plasticity, electron microscopy of synapses
MeSH terms: Animals, Brain, Cell Membrane, Models, Molecular, Nerve Tissue Proteins, Synapses, Receptors, Glutamate, Dendritic Spines

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The Postsynaptic Architecture of Excitatory Synapses: A More Quantitative View

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