Abstract
A new ionotropic glutamate receptor subunit termed KA-2, cloned from rat brain cDNA, exhibits high affinity for [ 3H]kainate (K D ≈ 15 nM). KA-2 mRNA is widely expressed in embryonic and adult brain. Homomeric KA-2 expression does not generate agonist-sensitive channels, but currents are observed when KA-2 is coexpressed with GluR5 or GIuR6 subunits. Specifically, coexpression of GluR5(R) and KA-2 produces channel activity, whereas homomeric expression of either subunit does not. Currents through heteromeric GluR5(Q)/KA-2 channels show more rapid desensitization and different current-voltage relations when compared with GIuR5(Q) currents. GluR6/KA-2 channels are gated by AMPA, which fails to gate homomeric GIuR6 receptor channels. These results suggest possible in vivo partnership relations for high affinity kainate receptors.
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