Identification of a Ca2+/calmodulin-dependent protein kinase II regulatory phosphorylation site in non-N-methyl-D-aspartate glutamate receptors

Jerrel L. Yakel, Prabhakar Vissavajjhala, Victor A. Derkach, Debra A. Brickey, Thomas R. Soderling

    Research output: Contribution to journalArticle

    88 Scopus citations

    Abstract

    Glutamate receptor ion channels are colocalized in postsynaptic densities with Ca2+/calmodulin-dependent protein kinase II (CaM-kinase II), which can phosphorylate and strongly enhance non-N-methyl-D-aspartate (NMDA) glutamate receptor current. In this study, CaM-kinase II enhanced kainate currents of expressed glutamate receptor 6 in 293 cells and of wild-type glutamate receptor 1, but not the Ser-627 to Ala mutant, in Xenopus oocytes. A synthetic peptide corresponding to residues 620-638 in GluR1 was phosphorylated in vitro by CaM-kinase II but not by cAMP-dependent protein kinase or protein kinase C. The 32P-labeled peptide map of this synthetic peptide appears to be the same as the two-dimensional peptide map of α-amino-3-hydroxy-5-methyl-4-isoxazole propionate (AMPA) glutamate receptors phosphorylated in cultured hippocampal neurons by CaM-kinase II described elsewhere. This CaM-kinase II regulatory phosphorylation site is conserved in all AMPA/ kainate-type glutamate receptors, and its phosphorylation may be important in enhancing postsynaptic responsiveness as occurs during synaptic plasticity.

    Original languageEnglish (US)
    Pages (from-to)1376-1380
    Number of pages5
    JournalProceedings of the National Academy of Sciences of the United States of America
    Volume92
    Issue number5
    DOIs
    StatePublished - Feb 28 1995

    Keywords

    • Ligand-gated ion channel
    • Patch clamp
    • Protein phosphorylation
    • Xenopus oocytes

    ASJC Scopus subject areas

    • General

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