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- Title
CaMKII phosphorylation of neuroligin-1 regulates excitatory synapses.
- Authors
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
- 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 Ca2+/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.
- Subjects
NEURAL circuitry; NEURAL transmission; NEUREXINS; HEMIDESMOSOMES; DESMOSOMES
- Publication
Nature Neuroscience, 2014, Vol 17, Issue 1, p56
- ISSN
1097-6256
- Publication type
Article
- DOI
10.1038/nn.3601