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Inhibitory autophosphorylation of CaMKII controls PSD association, plasticity, and learning.


To investigate the function of the alpha calcium-calmodulin-dependent kinase II (alphaCaMKII) inhibitory autophosphorylation at threonines 305 and/or 306, we generated knockin mice that express alphaCaMKII that cannot undergo inhibitory phosphorylation. In addition, we generated mice that express the inhibited form of alphaCaMKII, which resembles the persistently phosphorylated kinase at these sites. Our data demonstrate that blocking inhibitory phosphorylation increases CaMKII in the postsynaptic density (PSD), lowers the threshold for hippocampal long-term potentiation (LTP), and results in hippocampal-dependent learning that seems more rigid and less fine-tuned. Mimicking inhibitory phosphorylation dramatically decreased the association of CaMKII with the PSD and blocked both LTP and learning. These data demonstrate that inhibitory phosphorylation has a critical role in plasticity and learning.

Pubmed ID: 12408851


  • Elgersma Y
  • Fedorov NB
  • Ikonen S
  • Choi ES
  • Elgersma M
  • Carvalho OM
  • Giese KP
  • Silva AJ



Publication Data

October 24, 2002

Associated Grants

  • Agency: NIA NIH HHS, Id: AG 13622

Mesh Terms

  • Animals
  • Calcium-Calmodulin-Dependent Protein Kinase Type 2
  • Calcium-Calmodulin-Dependent Protein Kinases
  • Electric Stimulation
  • Excitatory Amino Acid Antagonists
  • Female
  • Gene Expression Regulation, Enzymologic
  • Hippocampus
  • Learning
  • Long-Term Potentiation
  • Long-Term Synaptic Depression
  • Male
  • Maze Learning
  • Membrane Potentials
  • Mice
  • Mice, Transgenic
  • Organ Culture Techniques
  • Phosphorylation
  • Presynaptic Terminals
  • Synaptic Membranes
  • Synaptic Transmission