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Volume 17, Number 20,
Issue of October 15, 1997
pp. 7634-7643
Copyright ©1997 Society for Neuroscience
Kainate Binding Proteins Possess Functional Ion Channel
Domains
Received June 16, 1997; revised July 28, 1997; accepted July 29, 1997.
Carmen Villmann,
Leonard Bull, and
Michael Hollmann
Glutamate Receptor Laboratory, Max-Planck-Institute for
Experimental Medicine, D-37075 Göttingen, Germany
Kainate binding proteins (KBPs) are highly homologous to ionotropic
glutamate receptors; however, no ion channel function has been
demonstrated for these proteins. To investigate possible reasons for
the apparent lack of ion channel function we transplanted the ion
channel domains of five KBPs into glutamate receptors GluR 6 and GluR1.
In each case we obtained functional chimeric receptors in which
glutamatergic agonists were able to open the KBP-derived ion channel
with EC50 values identical to those of the subunit
contributing the ligand binding domain. Maximal current amplitudes were
significantly smaller than those of the parent clones, however. We also
show that the KBP ion channels are highly permeable for calcium and
have certain pharmacological properties that are distinct from all
other glutamate receptor (GluR) subunits. Thus, all five known KBPs, in
addition to their well characterized functional ligand binding sites,
have functional ion permeation pathways. Our data suggest that the lack
of ion channel function in wild-type KBPs results from a failure to
translate ligand binding into channel opening. We interpret our
findings to indicate the requirement for a modulatory protein or an
additional subunit serving to alter the structure of the KBP subunit
complex such that signal transduction is enabled from the ligand
binding site to the intrinsically functional ion pore.
Key words:
kainate binding proteins;
KBP;
ion pore;
domain
transplantation;
kainate receptors;
GluR1;
GluR6;
calcium permeability;
Xenopus oocytes
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