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Local palmitoylation cycles define activity-regulated postsynaptic subdomains
Open accessAbstract
Distinct PSD-95 clusters are primary landmarks of postsynaptic densities (PSDs), which are specialized membrane regions for synapses. However, the mechanism that defines the locations of PSD-95 clusters and whether or how they are reorganized inside individual dendritic spines remains controversial. Because palmitoylation regulates PSD-95 membrane targeting, we combined a conformation-specific recombinant antibody against palmitoylated PSD-95 with live-cell super-resolution imaging and discovered subsynaptic nanodomains composed of palmitoylated PSD-95 that serve as elementary units of the PSD. PSD-95 in nanodomains underwent continuous de/repalmitoylation cycles driven by local palmitoylating activity, ensuring the maintenance of compartmentalized PSD-95 clusters within individual spines. Plasma membrane targeting of DHHC2 palmitoyltransferase rapidly recruited PSD-95 to the plasma membrane and proved essential for postsynaptic nanodomain formation. Furthermore, changes in synaptic activity rapidly reorganized PSD-95 nano-architecture through plasma membrane-inserted DHHC2. Thus, the first genetically encoded antibody sensitive to palmitoylation reveals an instructive role of local palmitoylation machinery in creating activity-responsive PSD-95 nanodomains, contributing to the PSD (re)organization.
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“The average estimated diameter of ~80 nm for RIM1/2 NCs was very close to the reported size of PSD-95 and AMPA receptor (AMPAR) NCs4–6.”
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“These presynaptic RIM nanoclusters closely aligned with concentrated postsynaptic receptors and scaffolding proteins4–6, suggesting a transsynaptic molecular “nanocolumn.””
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“The alignment of pre and postsynaptic nanoscale subdomains4–6 suggests that even small synapses may be composed of dynamic functional modules28,29.”
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Metadata
- Authors
- Fukata, Y., Dimitrov, A., Boncompain, G., Vielemeyer, O., Perez, F., & Fukata, M.
- Affiliations
- National Institute for Physiological Sciences (JP)
- Centre National de la Recherche Scientifique (FR)
- Centre National de la Recherche Scientifique, Unité Mixte de Recherche 144 2 and 3
- Corresponding author
- Perez, Franck
- Fukata, Masaki
- Venue
- Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2013-07-08
- Volume
- 202
- Issue
- 1
- Pages
- 145-161
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC3704990
- OpenAlex
- W2168234829
- Cited by
- 262
- References
- 58
- Citations by year
- 2026: 8 · 2025: 13 · 2024: 23 · 2023: 12 · 2022: 20 · 2021: 28 · 2020: 24 · 2019: 21 · 2018: 23 · 2017: 27 · 2016: 20 · 2015: 20 · 2014: 17 · 2013: 6
- FWCI
- 10.31
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by-nc-sa
- Locations
- The Journal of Cell Biology (publishedVersion, cc-by-nc-sa)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Funders
- Agence Nationale de la Recherche (ANR-09-BLAN-0290)
- Japan Society for the Promotion of Science
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Keywords
- palmitoylation, PSD-95, postsynaptic density, dendritic spines, plasma membrane targeting, synaptic organization
- MeSH terms
- Disks Large Homolog 4 Protein, Animals, Chlorocebus aethiops, Fluorescent Dyes, Hippocampus, Humans, Membrane Proteins, Synaptic Transmission, Neuronal Plasticity, Neurons, Palmitates, Sensitivity and Specificity, Structure-Activity Relationship, Transfection, COS Cells, Dendritic Spines, Green Fluorescent Proteins, Mice, Rats, Guanylate Kinases, Lipoylation, HEK293 Cells, Post-Synaptic Density
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