AIDA-1 Moves out of the Postsynaptic Density Core under Excitatory Conditions.

PLoS One

EM Facility, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, Maryland, United States of America.

Published: May 2016

AI Article Synopsis

  • AIDA-1 is a key protein found in the postsynaptic density (PSD) of neurons, and its localization and behavior during neuronal activity were examined using immunogold electron microscopy in rat hippocampal neurons.
  • Under normal conditions, AIDA-1 is concentrated within the dense core of the PSD, but during excitatory stimulation, its density decreases significantly, and its distance from the postsynaptic membrane increases.
  • This reversible redistribution of AIDA-1, similar to another protein called SynGAP, suggests a mechanism for synaptic flexibility and potential modification by freeing up binding sites on PSD-95 for other proteins to attach.

Article Abstract

AIDA-1 is highly enriched in postsynaptic density (PSD) fractions and is considered a major component of the PSD complex. In the present study, immunogold electron microscopy was applied to determine localization as well as the activity-induced redistribution of AIDA-1 at the PSD using two antibodies that recognize two different epitopes. In cultured rat hippocampal neurons under basal conditions, immunogold label for AIDA-1 is mostly located within the dense core of the PSD, with a median distance of ~30 nm from the postsynaptic membrane. Under excitatory conditions, such as depolarization with high K+ (90 mM, 2 min) or application of NMDA (50 μM, 2 min), AIDA-1 label density at the PSD core is reduced to 40% of controls and the median distance of label from the postsynaptic membrane increases to ~55 nm. The effect of excitatory conditions on the postsynaptic distribution of AIDA-1 is reversed within 30 minutes after returning to control conditions. The reversible removal of AIDA-1 from the PSD core under excitatory conditions is similar to the redistribution of another abundant PSD protein, SynGAP. Both SynGAP-alpha1 and AIDA-1 are known to bind PSD-95. Activity-induced transient translocation of these abundant proteins from the PSD core could promote structural flexibility, vacate sites on PSD-95 for the insertion of other components and thus may create a window for synaptic modification.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4565644PMC
http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0137216PLOS

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