CaMKII phosphorylation of neuroligin-1 regulates excitatory synapses.

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 Neurosci

journal_title

Nature neuroscience

authors

Bemben MA,Shipman SL,Hirai T,Herring BE,Li Y,Badger JD 2nd,Nicoll RA,Diamond JS,Roche KW

doi

10.1038/nn.3601

subject

Has Abstract

pub_date

2014-01-01 00:00:00

pages

56-64

issue

1

eissn

1097-6256

issn

1546-1726

pii

nn.3601

journal_volume

17

pub_type

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