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Related Experiment Video

Updated: May 9, 2026

Detection of Protein Palmitoylation in Cultured Hippocampal Neurons by Immunoprecipitation and Acyl-Biotin Exchange (ABE)

Detection of Protein Palmitoylation in Cultured Hippocampal Neurons by Immunoprecipitation and Acyl-Biotin Exchange (ABE)

Published on: February 18, 2013

Local palmitoylation cycles define activity-regulated postsynaptic subdomains.

Yuko Fukata¹, Ariane Dimitrov, Gaelle Boncompain

¹Division of Membrane Physiology, Department of Cell Physiology, National Institute for Physiological Sciences, Okazaki, Aichi 444-8787, Japan.

The Journal of Cell Biology

|July 10, 2013

Summary

Researchers discovered novel subsynaptic nanodomains of palmitoylated postsynaptic density-95 (PSD-95) that act as fundamental units of the postsynaptic density. Local palmitoylation machinery drives PSD-95 reorganization within dendritic spines, responding to synaptic activity.

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Last Updated: May 9, 2026

Detection of Protein Palmitoylation in Cultured Hippocampal Neurons by Immunoprecipitation and Acyl-Biotin Exchange (ABE)

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Area of Science:

Neuroscience
Molecular Biology
Cell Biology

Background:

Postsynaptic densities (PSDs) are crucial for synaptic function.
The precise organization and regulation of PSD-95 clusters within dendritic spines remain unclear.

Purpose of the Study:

To investigate the mechanism defining PSD-95 cluster locations.
To explore the dynamic reorganization of PSD-95 within dendritic spines.

Main Methods:

Utilized a conformation-specific antibody for palmitoylated PSD-95.
Employed live-cell super-resolution imaging techniques.
Investigated the role of DHHC2 palmitoyltransferase.

Main Results:

Identified subsynaptic nanodomains of palmitoylated PSD-95 as elementary PSD units.
Demonstrated continuous de/repalmitoylation cycles maintaining PSD-95 clusters.
Showed DHHC2 is essential for nanodomain formation and PSD-95 recruitment.
Revealed activity-dependent reorganization of PSD-95 nano-architecture via DHHC2.

Conclusions:

Local palmitoylation machinery dictates PSD-95 nanodomain formation and organization.
Palmitoylation-dependent nanodomains are activity-responsive and crucial for PSD structure.
The study provides insights into synaptic plasticity and structural regulation.