Glutamate receptors localize postsynaptically at neuromuscular junctions in mice

Authors

  • Tessily A. Mays BS,

    1. Department of Molecular and Cellular Biochemistry, 410 Hamilton Hall, College of Medicine, Ohio State University, 1645 Neil Avenue, Columbus, Ohio 43210, USA
    Search for more papers by this author
  • Jamie L. Sanford PhD,

    1. Department of Molecular and Cellular Biochemistry, 410 Hamilton Hall, College of Medicine, Ohio State University, 1645 Neil Avenue, Columbus, Ohio 43210, USA
    Search for more papers by this author
  • Toshihiko Hanada PhD,

    1. Department of Pharmacology, UIC Cancer Center, University of Illinois College of Medicine, Chicago, Illinois, USA
    Search for more papers by this author
  • Athar H. Chishti PhD,

    1. Department of Pharmacology, UIC Cancer Center, University of Illinois College of Medicine, Chicago, Illinois, USA
    Search for more papers by this author
  • Jill A. Rafael-Fortney PhD

    Corresponding author
    1. Department of Molecular and Cellular Biochemistry, 410 Hamilton Hall, College of Medicine, Ohio State University, 1645 Neil Avenue, Columbus, Ohio 43210, USA
    • Department of Molecular and Cellular Biochemistry, 410 Hamilton Hall, College of Medicine, Ohio State University, 1645 Neil Avenue, Columbus, Ohio 43210, USA
    Search for more papers by this author

Abstract

Dlg (Discs Large) is a multidomain protein that interacts with glutamate receptors and potassium channels at Drosophila neuromuscular junctions (NMJs) and at mammalian central nervous system synapses. Dlg also localizes postsynaptically at cholinergic mammalian NMJs. We show here that α-amino-3-hydroxy-5-methylisoxazole-4-proprionate (AMPA) receptor subunits, together with glutamate, are present at the mammalian NMJ. Both AMPA and NMDA (N-methyl-D-aspartate) glutamate receptor subunits display overlapping postsynaptic localization patterns with Dlg at all NMJs examined in normal mice. Kir2 potassium channels also localize with Dlg and glutamate receptors at this synapse. Localization of the components of a glutamatergic system suggests novel mechanisms at mammalian neuromuscular synapses. Muscle Nerve 39: 343–349, 2009

Ancillary