Structural plasticity with preserved topology in the postsynaptic protein network.
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.
Blanpied
Thomas A
TA
Department of Neurobiology, Duke University Medical Center, Durham, NC 27710, USA. tblanpied@som.umaryland.edu
Kerr
Justin M
JM
Ehlers
Michael D
MD
D000818:Animals; D002478:Cells, Cultured; D003599:Cytoskeleton; D049229:Dendritic Spines; D003952:Diagnostic Imaging; D000076122:Disks Large Homolog 4 Protein; D049452:Green Fluorescent Proteins; D006624:Hippocampus / Q000166:cytology; D047908:Intracellular Signaling Peptides and Proteins / Q000032:analysis*; D008565:Membrane Proteins / Q000032:analysis*; D008954:Models, Biological; D009419:Nerve Tissue Proteins; D009474:Neurons / Q000166:cytology*; D051381:Rats; D013569:Synapses / Q000737:chemistry / Q000648:ultrastructure*
D000076122:Disks Large Homolog 4 Protein; C501449:Dlg4 protein, rat; D047908:Intracellular Signaling Peptides and Proteins; D008565:Membrane Proteins; D009419:Nerve Tissue Proteins; C033652:postsynaptic density proteins; D049452:Green Fluorescent Proteins