Identification of the Ca2+/calmodulin-dependent protein kinase II regulatory phosphorylation site in the α-amino-3-hydroxyl-5-methyl-4- isoxazole-propionate-type glutamate receptor

Andres Barria, Victor Derkach, Thomas Soderling

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    302 Scopus citations

    Abstract

    Ca2+/CaM-dependent protein kinase II (CaM-KII) can phosphorylate and potentiate responses of α-amino-3-hydroxyl-5-methyl-4-isoxazole-propionate- type glutamate receptors in a number of systems, and recent studies implicate this mechanism in long term potentiation, a cellular model of learning and memory. In this study we have identified this CaM-KII regulatory site using deletion and site-specific mutants of glutamate receptor 1 (GIuR1). Only mutations affecting Set831 altered the 32P peptide maps of GluR1 from HEK-293 cells co- expressing an activated CaM-KII. Likewise, when CaM-KII was infused into cells expressing GluR1, the Ser831 to Ala mutant failed to show potentiation of the GluR1 current. The Ser831 site is specific to GluR1, and CaM-KII did not phosphorylate or potentiate current in cells expressing GluR2, emphasizing the importance of the GluR1 subunit in this regulatory mechanism. Because Set831 has previously been identified as a protein kinase C phosphorylation site (Roche. K. W., O'Brien, R. J., Mammen, A. L., Bernhardt, J., and Huganir, R. L. (1996) Neuron 16, 1179-1188), this raises the possibility of synergistic interactions between CaM-KII and protein kinase C in regulating synaptic plasticity.

    Original languageEnglish (US)
    Pages (from-to)32727-32730
    Number of pages4
    JournalJournal of Biological Chemistry
    Volume272
    Issue number52
    DOIs
    StatePublished - Dec 26 1997

    ASJC Scopus subject areas

    • Biochemistry
    • Molecular Biology
    • Cell Biology

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