Synaptic accumulation of PSD-95 and synaptic function regulated by phosphorylation of serine-295 of PSD-95

Neuron. 2007 Nov 8;56(3):488-502. doi: 10.1016/j.neuron.2007.09.007.

Abstract

The scaffold protein PSD-95 promotes the maturation and strengthening of excitatory synapses, functions that require proper localization of PSD-95 in the postsynaptic density (PSD). Here we report that phosphorylation of ser-295 enhances the synaptic accumulation of PSD-95 and the ability of PSD-95 to recruit surface AMPA receptors and potentiate excitatory postsynaptic currents. We present evidence that a Rac1-JNK1 signaling pathway mediates ser-295 phosphorylation and regulates synaptic content of PSD-95. Ser-295 phosphorylation is suppressed by chronic elevation, and increased by chronic silencing, of synaptic activity. Rapid dephosphorylation of ser-295 occurs in response to NMDA treatment that causes chemical long-term depression (LTD). Overexpression of a phosphomimicking mutant (S295D) of PSD-95 inhibited NMDA-induced AMPA receptor internalization and blocked the induction of LTD. The data suggest that synaptic strength can be regulated by phosphorylation-dephosphorylation of ser-295 of PSD-95 and that synaptic depression requires the dephosphorylation of ser-295.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Animals
  • Animals, Newborn
  • Cells, Cultured
  • Disks Large Homolog 4 Protein
  • Excitatory Amino Acid Agonists / pharmacology
  • Excitatory Postsynaptic Potentials / physiology
  • Hippocampus / metabolism*
  • Hippocampus / ultrastructure
  • Intracellular Signaling Peptides and Proteins / chemistry
  • Intracellular Signaling Peptides and Proteins / genetics
  • Intracellular Signaling Peptides and Proteins / metabolism*
  • JNK Mitogen-Activated Protein Kinases / metabolism
  • Long-Term Synaptic Depression / drug effects
  • Long-Term Synaptic Depression / physiology
  • Membrane Proteins / chemistry
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism*
  • Mutation / physiology
  • N-Methylaspartate / pharmacology
  • Organ Culture Techniques
  • Phosphorylation / drug effects
  • Rats
  • Receptors, AMPA / drug effects
  • Receptors, AMPA / metabolism
  • Serine / metabolism*
  • Signal Transduction / drug effects
  • Signal Transduction / physiology
  • Synaptic Membranes / drug effects
  • Synaptic Membranes / metabolism*
  • Synaptic Membranes / ultrastructure
  • Synaptic Transmission / drug effects
  • Synaptic Transmission / physiology*
  • rac1 GTP-Binding Protein / metabolism

Substances

  • Disks Large Homolog 4 Protein
  • Dlg4 protein, rat
  • Excitatory Amino Acid Agonists
  • Intracellular Signaling Peptides and Proteins
  • Membrane Proteins
  • Receptors, AMPA
  • Serine
  • N-Methylaspartate
  • JNK Mitogen-Activated Protein Kinases
  • rac1 GTP-Binding Protein