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.
journal_name
Nat Neuroscijournal_title
Nature neuroscienceauthors
Bemben MA,Shipman SL,Hirai T,Herring BE,Li Y,Badger JD 2nd,Nicoll RA,Diamond JS,Roche KWdoi
10.1038/nn.3601subject
Has Abstractpub_date
2014-01-01 00:00:00pages
56-64issue
1eissn
1097-6256issn
1546-1726pii
nn.3601journal_volume
17pub_type
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