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Journal of Neuroscience, Vol 12, 4080-4087, Copyright © 1992 by Society for Neuroscience
Structural determinants of barium permeation and rectification in non- NMDA glutamate receptor channels
R Dingledine, RI Hume and SF Heinemann
Molecular Neurobiology Laboratory, Salk Institute, La Jolla, California 92037.
A single site in recombinant glutamate receptor channels of the GluR1-
GluR4 family has been previously identified as a key regulator of ion
permeation. The natural amino acid at this position (arginine in GluR2 but
glutamine in GluR1, GluR3, and GluR4) determines both the ability to pass
outward current and the divalent cation permeability of kainate- activated
receptor channels. By mutagenesis of GluR6, we demonstrated that the same
site also controls the ability to pass outward current in another non-NMDA
receptor family. Additional mutations at and near this site in GluR3
indicated that the position of the arginine is critical to function, that
the ability to pass outward current is not necessarily linked to low barium
permeability, and that the size as well as the charge of the side chain at
this position influences barium permeation. These results provide evidence
that this site forms part of the selectivity filter of glutamate receptor
channels.
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