Differential regulation of kainate receptor trafficking by phosphorylation of distinct sites on GluR6.

ABSTRACT: Kainate receptors are widely expressed in the brain, and are present at pre- and postsynaptic sites where they play a prominent role in synaptic plasticity and the regulation of network activity. Within individual neurons, kainate receptors of different subunit compositions are targeted to various locations where they serve distinct functional roles. Despite this complex targeting, relatively little is known about the molecular mechanisms regulating kainate receptor subunit trafficking. Here we investigate the role of phosphorylation in the trafficking of the GluR6 kainate receptor subunit. We identify two specific residues on the GluR6 C terminus, Ser(846) and Ser(868), which are phosphorylated by protein kinase C (PKC) and dramatically regulate GluR6 surface expression. By using GluR6 co

SUBMITTER: Nasu-Nishimura Y 

PROVIDER: S-EPMC2807338 | biostudies-literature | 2010 Jan

REPOSITORIES: biostudies-literature