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. 1994 Jul 19;91(15):7154-8.
doi: 10.1073/pnas.91.15.7154.

Transmembrane topology of two kainate receptor subunits revealed by N-glycosylation

Z G Wo  1 , R E Oswald
Affiliations

Transmembrane topology of two kainate receptor subunits revealed by N-glycosylation

Z G Wo et al. Proc Natl Acad Sci U S A. .

Abstract

Glutamate receptors are the primary excitatory neurotransmitter receptors in vertebrate brain and are of critical importance to a wide variety of neurological processes. Recent reports suggest that ionotropic glutamate receptors may have a unique transmembrane topology not shared by other ligand-gated ion channels. We report here the cloning of cDNAs from goldfish brain encoding two homologous kainate receptors with protein molecular masses of 41 kDa. Using a cell-free translation/translocation system, we show that (i) a portion of these receptors previously thought to be a large intracellular loop is actually located extracellularly and (ii) the putative second transmembrane region of the receptor thought to line the ion channel may not be a true membrane-spanning domain. An alternative model for the transmembrane topology of kainate receptors is proposed that could potentially serve as a framework for future detailed study of the structure of this important class of neurotransmitter receptors.

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