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Structural plasticity with preserved topology in the postsynaptic protein network.


ABSTRACT: The size, shape, and molecular arrangement of the postsynaptic density (PSD) determine the function of excitatory synapses in the brain. Here, we directly measured the internal dynamics of scaffold proteins within single living PSDs, focusing on the principal scaffold protein PSD-95. We found that individual PSDs undergo rapid, continuous changes in morphology driven by the actin cytoskeleton and regulated by synaptic activity. This structural plasticity is accompanied by rapid fluctuations in internal scaffold density over submicron distances. Using targeted photobleaching and photoactivation of PSD subregions, we show that PSD-95 is nearly immobile within the PSD, and PSD subdomains can be maintained over long periods. We propose a flexible matrix model of the PSD based on stable molecular positioning of PSD-95 scaffolds.

SUBMITTER: Blanpied TA 

PROVIDER: S-EPMC2519044 | biostudies-literature | 2008 Aug

REPOSITORIES: biostudies-literature

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Structural plasticity with preserved topology in the postsynaptic protein network.

Blanpied Thomas A TA   Kerr Justin M JM   Ehlers Michael D MD  

Proceedings of the National Academy of Sciences of the United States of America 20080822 34


The size, shape, and molecular arrangement of the postsynaptic density (PSD) determine the function of excitatory synapses in the brain. Here, we directly measured the internal dynamics of scaffold proteins within single living PSDs, focusing on the principal scaffold protein PSD-95. We found that individual PSDs undergo rapid, continuous changes in morphology driven by the actin cytoskeleton and regulated by synaptic activity. This structural plasticity is accompanied by rapid fluctuations in i  ...[more]

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