Organization of amyloid-b protein precursor intracellular domain-associated protein-1 in the rat brain

Amanda L. Jacob, Bryen A. Jordan, Richard J. Weinberg

Research output: Contribution to journalArticlepeer-review

17 Scopus citations


Sustained activity-dependent synaptic modifications require protein synthesis. Although proteins can be synthesized locally in dendrites, long-term changes also require nuclear signaling. Amyloid-β protein precursor intracellular domain-associated protein-1 (AIDA-1), an abundant component of the biochemical postsynaptic density fraction, contains a nuclear localization sequence, making it a plausible candidate for synapseto-nucleus signaling. We used immunohistochemistry to study the regional, cellular, and subcellular distribution of AIDA-1. Immunostaining was prominent in the hippocampus, cerebral cortex, and neostriatum. Along with diffuse staining of neuropil, fluorescence microscopy revealed immunostaining of excitatory synapses throughout the forebrain, and immunoreactive puncta within and directly outside the nucleus. Presynaptic staining was conspicuous in hippocampal mossy fibers. Electron microscopic analysis of material processed for postembedding immunogold revealed AIDA-1 label within postsynaptic densities in both hippocampus and cortex. Together with previous work, these data suggest that AIDA-1 serves as a direct signaling link between synapses and the nucleus in adult rat brain.

Original languageEnglish (US)
Pages (from-to)3221-3236
Number of pages16
JournalJournal of Comparative Neurology
Issue number16
StatePublished - Aug 15 2010


  • AICD
  • AIDA-1
  • APP
  • PSD
  • immunogold
  • synapse-to-nucleus signaling
  • synaptic plasticity

ASJC Scopus subject areas

  • General Neuroscience


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