A role for cGMP-dependent protein kinase II in AMPA receptor trafficking and synaptic plasticity
© Serulle et al; licensee BioMed Central Ltd. 2009
Published: 11 August 2009
Trafficking of AMPA receptors (AMPARs) underlies the activity-dependent modification of synaptic strength and is regulated by specific interactions of AMPAR subunits with other proteins. We have reported (Serulle et al., 2007)  that the AMPAR subunit GluR1 binds the cGMP-dependent kinase type II (cGKII) adjacent to the kinase catalytic site, and that this interaction is increased by cGMP. In this complex, cGKII phosphorylates GluR1 at serine 845 (S845) leading to an increase of GluR1 on the plasma membrane. In neurons, cGMP is produced by soluble guanylate cyclase (sGC), which is activated by nitric oxide (NO), which is produced by nNOS under the control of the NMDA receptor.
These data suggest that S845 phosphorylation increases the plasma membrane levels of GluR1 by reducing the rate of endocytosis.
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