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Related Experiment Videos

Glutamate receptor modulation by protein phosphorylation

L A Raymond1, W G Tingley, C D Blackstone

  • 1Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, MD 21205.

Journal of Physiology, Paris
|January 1, 1994
PubMed
Summary

Protein kinases directly phosphorylate glutamate receptors, altering their function. This study identifies specific phosphorylation sites on GluR6 and NR1 subunits, revealing insights into receptor modulation and structure.

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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Cell Biology

Background:

  • Glutamate receptors are crucial for excitatory neurotransmission and synaptic plasticity in the mammalian brain.
  • Protein phosphorylation by cyclic AMP-dependent protein kinase (PKA) and protein kinase C (PKC) is hypothesized to regulate glutamate receptor function.

Purpose of the Study:

  • To determine if PKA and PKC directly phosphorylate glutamate receptors.
  • To identify specific phosphorylation sites and elucidate the mechanisms of receptor modulation.
  • To investigate the impact of phosphorylation on receptor function and membrane topology.

Main Methods:

  • Transient expression of recombinant glutamate receptors (GluR6, NR1, NR2A) in HEK-293 cells.
  • Biochemical analysis to identify phosphorylation sites.

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  • Whole-cell patch-clamp recording to assess biophysical properties and current amplitudes.
  • Site-directed mutagenesis to examine the role of specific phosphorylation sites.

    • Main Results:

    • PKA directly phosphorylates the kainate receptor GluR6 at a single serine in the intracellular loop, increasing glutamate current amplitude.
    • PKC phosphorylates the NMDA receptor subunit NR1 at multiple sites within an alternatively spliced C-terminal exon.
    • Phosphorylation of NR1 suggests regulation by RNA splicing and an intracellular C-terminus, with PKC potentiating NMDA-evoked currents.

    Conclusions:

    • Glutamate receptors are directly phosphorylated and functionally modulated by PKA and PKC.
    • Identification of phosphorylation sites provides structural and topological information about glutamate receptors.
    • These findings advance the understanding of synaptic plasticity and potential neuropathological mechanisms involving glutamate receptor signaling.