To gate or not to gate: are the delta subunits in the glutamate receptor family functional ion channels? - PubMed (original) (raw)

Review

. 2008 Apr-Jun;37(2-3):126-41.

doi: 10.1007/s12035-008-8025-0. Epub 2008 Jun 3.

Affiliations

Review

To gate or not to gate: are the delta subunits in the glutamate receptor family functional ion channels?

Sabine M Schmid et al. Mol Neurobiol. 2008 Apr-Jun.

Abstract

The two delta receptor subunits remain the most puzzling enigma within the ionotropic glutamate receptor family. Despite the recent elucidation of the ligand-binding domain structure of delta2, many fundamental questions with regard to the subunits' mechanism of function still remain unanswered. Of necessity, the majority of studies on delta receptors focused on the metabotropic function of delta2, since electrophysiological approaches to date are limited to the characterization of spontaneous currents through the delta2-lurcher mutant. Indeed, accumulated evidence primarily from delta2-deficient transgenic mice suggest that major physiological roles of delta2 are mediated via metabotropic signaling by the subunit's C terminus. Why then would the subunits retain a conserved ion channel domain if they do not form functional ion channels? Any progress with regard to ionotropic function of the two delta subunits has been hampered by their largely unknown pharmacology. Even now that a pharmacological profile for delta2 is being established on the basis of the ligand-binding domain structure, wild-type delta2 channels in heterologous expression systems stay closed in the presence of molecules that have been demonstrated to bind to the receptor's ligand-binding domain. In this paper, we review the current knowledge of delta subunits focusing on the disputed ionotropic function.

PubMed Disclaimer

Similar articles

Cited by

References

    1. Biophys J. 1997 May;72(5):2103-16 - PubMed
    1. Brain Res Mol Brain Res. 2003 Jan 31;110(1):27-37 - PubMed
    1. Neuropharmacology. 1998 Oct-Nov;37(10-11):1321-34 - PubMed
    1. J Neurochem. 1997 Mar;68(3):1041-52 - PubMed
    1. Biochem Biophys Res Commun. 2000 Aug 28;275(2):565-71 - PubMed

Publication types

MeSH terms

Substances

LinkOut - more resources