Glutamate receptors localize postsynaptically at neuromuscular junctions in mice.
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 alpha-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.
Mays
Tessily A
TA
Department of Molecular and Cellular Biochemistry, 410 Hamilton Hall, College of Medicine, Ohio State University, 1645 Neil Avenue, Columbus, Ohio 43210, USA.
Sanford
Jamie L
JL
Hanada
Toshihiko
T
Chishti
Athar H
AH
Rafael-Fortney
Jill A
JA
D000818:Animals; D002038:Bungarotoxins / Q000378:metabolism; D018698:Glutamic Acid; D051379:Mice; D008810:Mice, Inbred C57BL; D018613:Microscopy, Confocal / Q000379:methods; D008856:Microscopy, Fluorescence; D009419:Nerve Tissue Proteins / Q000378:metabolism; D009469:Neuromuscular Junction / Q000166:cytology / Q000378:metabolism*; D015221:Potassium Channels / Q000378:metabolism; D017470:Receptors, Glutamate / Q000145:classification* / Q000378:metabolism*; D000074407:SAP90-PSD95 Associated Proteins; D015222:Sodium Channels / Q000378:metabolism; D013570:Synaptic Membranes / Q000378:metabolism*; D016708:Synaptophysin / Q000378:metabolism
D002038:Bungarotoxins; D009419:Nerve Tissue Proteins; D015221:Potassium Channels; D017470:Receptors, Glutamate; D000074407:SAP90-PSD95 Associated Proteins; D015222:Sodium Channels; D016708:Synaptophysin; D018698:Glutamic Acid