| First Author | Bemben MA | Year | 2014 |
| Journal | Nat Neurosci | Volume | 17 |
| Issue | 1 | Pages | 56-64 |
| PubMed ID | 24336150 | Mgi Jnum | J:208022 |
| Mgi Id | MGI:5560436 | Doi | 10.1038/nn.3601 |
| Citation | Bemben MA, et al. (2014) CaMKII phosphorylation of neuroligin-1 regulates excitatory synapses. Nat Neurosci 17(1):56-64 |
| abstractText | 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. |
