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Molecular Pharmacology, Volume 52, Issue 5, 861-873
Glutamate Receptor Laboratory, Max-Planck-Institute for Experimental Medicine, D-37075 Göttingen, Germany
All ionotropic glutamate receptor (iGluR) subunits analyzed so far are
heavily N-glycosylated at multiple sites on their
amino-terminal extracellular domains. Although the exact functional
significance of this glycosylation remains to be determined, it has
been suggested that N-glycosylation may be a
precondition for the formation of functional ion channels. In
particular, it has been argued that N-glycosylation is
required for the formation of functional ligand binding sites. We
analyzed heterologously expressed recombinant glutamate receptors
(GluRs) of all three pharmacological subclasses of glutamate receptors,
N-methyl-D-aspartate (NMDA),
-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid, and kainate
receptors. By expressing the GluR subunits in tunicamycin-treated,
nonglycosylating Xenopus laevis oocytes, we determined
that in neither case is N-glycosylation required for ion
channel function, although for NMDA receptors, functional expression in
the absence of N-glycosylation is very low. Furthermore,
we analyzed and compared the interaction of the
desensitization-inhibiting lectin concanavalin A (ConA) with all
functional GluR subunits. We show that although ConA has its most
pronounced effects on kainate receptors, it potentiates currents at
most other receptor subtypes as well, including certain NMDA receptor
subunits, although to a much lesser extent. One notable exception is
the -amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptor
GluR2, which is not affected by ConA. Furthermore, we show that ConA
acts directly via binding to the carbohydrate side chains of the
receptor protein.
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