We have updated our privacy policy. If you have any question, contact us at privacy@scicrunch.org. Dismiss and don't show again

Searching across hundreds of databases

Our searching services are busy right now. Your search will reload in five seconds.

Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

CaMKII phosphorylation of neuroligin-1 regulates excitatory synapses.

Nature neuroscience | Jan 26, 2014

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.

Pubmed ID: 24336150 RIS Download

Mesh terms: Animals | Animals, Newborn | Benzylamines | Bicuculline | Calcium-Calmodulin-Dependent Protein Kinase Type 2 | Cell Adhesion Molecules, Neuronal | Cells, Cultured | Dose-Response Relationship, Drug | Electric Stimulation | Excitatory Amino Acid Antagonists | Excitatory Postsynaptic Potentials | Female | GABA Antagonists | Gene Expression Regulation | Guanylate Kinases | Hippocampus | Humans | Immunoprecipitation | In Vitro Techniques | Luminescent Proteins | Male | Mass Spectrometry | Membrane Proteins | Mice | Mice, Inbred C57BL | MicroRNAs | Mutation | Neurons | Patch-Clamp Techniques | Phosphorylation | Protein Kinase Inhibitors | Receptors, AMPA | Sensory Deprivation | Sequence Analysis, Protein | Statistics, Nonparametric | Sulfonamides | Synapses | Transfection | Vesicular Glutamate Transport Protein 1 | Visual Cortex

Research tools detected in this publication

None found

Data used in this publication

None found

Associated grants

  • Agency: NIMH NIH HHS, Id: R37 MH038256
  • Agency: NIMH NIH HHS, Id: 5 R37 MH038256
  • Agency: Intramural NIH HHS, Id:

Publication data is provided by the National Library of Medicine ® and PubMed ®. Data is retrieved from PubMed ® on a weekly schedule. For terms and conditions see the National Library of Medicine Terms and Conditions.