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 Soderling

    Research output: Contribution to journalArticle

    87 Citations (Scopus)

    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
    StatePublished - Feb 28 1995

    Fingerprint

    D-Aspartic Acid
    Calcium-Calmodulin-Dependent Protein Kinase Type 2
    Glutamate Receptors
    Phosphorylation
    Peptides
    Isoxazoles
    Post-Synaptic Density
    Kainic Acid Receptors
    alpha-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid
    Neuronal Plasticity
    AMPA Receptors
    Kainic Acid
    Propionates
    Xenopus
    Cyclic AMP-Dependent Protein Kinases
    Ion Channels
    Protein Kinase C
    Oocytes
    aspartic acid receptor
    Neurons

    Keywords

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

    ASJC Scopus subject areas

    • General
    • Genetics

    Cite this

    Identification of a Ca2+/calmodulin-dependent protein kinase II regulatory phosphorylation site in non-N-methyl-D-aspartate glutamate receptors. / Yakel, Jerrel L.; Vissavajjhala, Prabhakar; Derkach, Victor A.; Brickey, Debra A.; Soderling, Thomas.

    In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 92, No. 5, 28.02.1995, p. 1376-1380.

    Research output: Contribution to journalArticle

    Yakel, Jerrel L. ; Vissavajjhala, Prabhakar ; Derkach, Victor A. ; Brickey, Debra A. ; Soderling, Thomas. / Identification of a Ca2+/calmodulin-dependent protein kinase II regulatory phosphorylation site in non-N-methyl-D-aspartate glutamate receptors. In: Proceedings of the National Academy of Sciences of the United States of America. 1995 ; Vol. 92, No. 5. pp. 1376-1380.
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