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CaMKII phosphorylation of neuroligin-1 regulates excitatory synapses.

  • Author(s): Bemben, Michael A
  • Shipman, Seth L
  • Hirai, Takaaki
  • Herring, Bruce E
  • Li, Yan
  • Badger, John D
  • Nicoll, Roger A
  • Diamond, Jeffrey S
  • Roche, Katherine W
  • et al.

Published Web Location

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3943352/
No data is associated with this publication.
Abstract

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.

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