Centaurin-α1-Ras-Elk-1 signaling at mitochondria mediates β-amyloid-induced synaptic dysfunction

J Neurosci. 2013 Mar 20;33(12):5367-74. doi: 10.1523/JNEUROSCI.2641-12.2013.

Abstract

Alzheimer's disease is thought to be caused by β-amyloid peptide (Aβ)-dependent synaptic dysfunction. However, the signaling pathways connecting Aβ and synaptic dysfunction remain elusive. Here we report that Aβ transiently increases the expression level of centaurin-α1 (CentA1) in neurons, which induces a Ras-dependent association of Elk-1 with mitochondria, leading to mitochondrial and synaptic dysfunction in organotypic hippocampal slices of rats. Downregulation of the CentA1-Ras-Elk-1 pathway restored normal mitochondrial activity, spine structural plasticity, spine density, and the amplitude and frequency of miniature EPSCs in Aβ-treated neurons, whereas upregulation of the pathway was sufficient to decrease spine density. Elevations of CentA1 and association of Elk-1 with mitochondria were also observed in transgenic mice overexpressing a human mutant form of amyloid precursor protein. Therefore, the CentA1-Ras-Elk-1 signaling pathway acts on mitochondria to regulate dendritic spine density and synaptic plasticity in response to Aβ in hippocampal neurons, providing new pharmacological targets for Alzheimer's disease.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alzheimer Disease / metabolism*
  • Alzheimer Disease / pathology
  • Amyloid beta-Peptides / metabolism*
  • Animals
  • Cells, Cultured
  • Dendritic Spines / metabolism
  • Dendritic Spines / pathology
  • Excitatory Postsynaptic Potentials / physiology
  • GTPase-Activating Proteins / metabolism*
  • Hippocampus / cytology
  • Humans
  • MAP Kinase Signaling System / physiology*
  • Male
  • Mice
  • Mice, Inbred Strains
  • Mice, Transgenic
  • Mitochondria / metabolism
  • Nerve Tissue Proteins / metabolism*
  • Neuronal Plasticity / physiology
  • Neurons / cytology
  • Neurons / physiology
  • Rats
  • Rats, Sprague-Dawley
  • Synapses / metabolism
  • Synapses / pathology
  • ets-Domain Protein Elk-1 / metabolism*
  • ras Proteins / metabolism*

Substances

  • Adap1 protein, rat
  • Amyloid beta-Peptides
  • Elk1 protein, mouse
  • Elk1 protein, rat
  • GTPase-Activating Proteins
  • Nerve Tissue Proteins
  • ets-Domain Protein Elk-1
  • ras Proteins