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Science 21 June 1991: Vol. 252. no. 5013, pp. 1715 - 1718 DOI: 10.1126/science.1710829
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Articles
Science, Vol 252, Issue 5013, 1715-1718
Copyright © 1991 by American Association for the Advancement of Science
Structural determinants of ion flow through recombinant glutamate receptor channels
TA Verdoorn,
N Burnashev,
H Monyer,
PH Seeburg,
and
B Sakmann
Max-Planck-Institut fur medizinische Forschung, Abteilung Zellphysiologie, Heidelberg, Federal Republic of Germany.
Functional glutamate receptor (GluRs) were transiently expressed in cultured mammalian cells from cloned complementary DNAs encoding GluR-A, -B, -C, or -D polypeptides. The steady-state current-voltage (I-V) relations of glutamate- and kainate-induced currents through homomeric channels fell into two classes: channels composed of either the GluR-A, -C, and -D subunits showed doubly rectifying I-V curves, and channels composed of the GluR-B subunits displayed simple outward rectification. The presence of GluR-B subunits in heteromeric GluRs determined the I-V behavior of the resulting channels. Site-directed mutagenesis identified a single amino acid difference (glutamine to arginine) in the putative transmembrane segment TM2 responsible for subunit-specific I-V relationships. The properties of heteromeric wild-type and mutant GluRs revealed that the dominance of GluR-B is due to the arginine residue in the TM2 region.
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