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CaMKII phosphorylation of neuroligin-1 regulates excitatory synapses.

Neuroligins are postsynaptic cell adhesion molecules that are important for synaptic function through their trans-synaptic interaction with neurexins (NRXNs). The localization and synaptic effects of neuroligin-1 (NL-1, also called NLGN1) are specific to excitatory synapses with the capacity to enhance excitatory synapses dependent on synaptic activity or Ca(2+)/calmodulin kinase II (CaMKII). Here we report that CaMKII robustly phosphorylates the intracellular domain of NL-1. We show that T739 is the dominant CaMKII site on NL-1 and is phosphorylated in response to synaptic activity in cultured rodent neurons and sensory experience in vivo. Furthermore, a phosphodeficient mutant (NL-1 T739A) reduces the basal and activity-driven surface expression of NL-1, leading to a reduction in neuroligin-mediated excitatory synaptic potentiation. To the best of our knowledge, our results are the first to demonstrate a direct functional interaction between CaMKII and NL-1, two primary components of excitatory synapses.

Pubmed ID: 24336150


  • Bemben MA
  • Shipman SL
  • Hirai T
  • Herring BE
  • Li Y
  • Badger JD
  • Nicoll RA
  • Diamond JS
  • Roche KW


Nature neuroscience

Publication Data

January 26, 2014

Associated Grants

  • Agency: NIMH NIH HHS, Id: 5 R37 MH038256
  • Agency: NIMH NIH HHS, Id: R37 MH038256
  • Agency: Intramural NIH HHS, Id:

Mesh Terms

  • Animals
  • Animals, Newborn
  • Benzylamines
  • Bicuculline
  • Calcium-Calmodulin-Dependent Protein Kinase Type 2
  • Cell Adhesion Molecules, Neuronal
  • Cells, Cultured
  • Dose-Response Relationship, Drug
  • Electric Stimulation
  • Excitatory Amino Acid Antagonists
  • Excitatory Postsynaptic Potentials
  • Female
  • GABA Antagonists
  • Gene Expression Regulation
  • Guanylate Kinase
  • Hippocampus
  • Humans
  • Immunoprecipitation
  • In Vitro Techniques
  • Luminescent Proteins
  • Male
  • Mass Spectrometry
  • Membrane Proteins
  • Mice
  • Mice, Inbred C57BL
  • MicroRNAs
  • Mutation
  • Neurons
  • Patch-Clamp Techniques
  • Phosphorylation
  • Protein Kinase Inhibitors
  • Receptors, AMPA
  • Sensory Deprivation
  • Sequence Analysis, Protein
  • Statistics, Nonparametric
  • Sulfonamides
  • Synapses
  • Transfection
  • Vesicular Glutamate Transport Protein 1
  • Visual Cortex