Alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptor channels lacking the N-terminal domain.

Pasternack, A., Coleman, S.K., Jouppila, A., Mottershead, D.G., Lindfors, M., Pasternack, M. and Keinänen, K. 2002. Alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptor channels lacking the N-terminal domain. Journal of Biological Chemistry. 277 (51), pp. P49662-49667. https://doi.org/10.1074/jbc.m208349200

TitleAlpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptor channels lacking the N-terminal domain.
TypeJournal article
AuthorsPasternack, A., Coleman, S.K., Jouppila, A., Mottershead, D.G., Lindfors, M., Pasternack, M. and Keinänen, K.
Abstract

Ionotropic glutamate receptor (iGluR) subunits contain a ∼400-residue extracellular N-terminal domain (“X domain”), which is sequence-related to bacterial amino acid-binding proteins and to class C G-protein-coupled receptors. The X domain has been implicated in the assembly, transport to the cell surface, allosteric ligand binding, and desensitization in various members of the iGluR family, but its actual role in these events is poorly characterized. We have studied the properties of homomeric α-amino-3-hydroxy-5-methylisoxazolepropionate (AMPA)-selective GluR-D glutamate receptors carrying N-terminal deletions. Our analysis indicates that, surprisingly, transport to the cell surface, ligand binding properties, agonist-triggered channel activation, rapid desensitization, and allosteric potentiation by cyclothiazide can occur normally in the complete absence of the X domain (residues 22–402). The relatively intact ligand-gated channel function of a homomeric AMPA receptor in the absence of the X domain indirectly suggests more subtle roles for this domain in AMPA receptors, e.g. in the assembly of heteromeric receptors and in synaptic protein interactions.

JournalJournal of Biological Chemistry
Journal citation277 (51), pp. P49662-49667
ISSN0021-9258
1083-351X
Year2002
PublisherElsevier
Publisher's version
License
CC BY 4.0
File Access Level
Open (open metadata and files)
Digital Object Identifier (DOI)https://doi.org/10.1074/jbc.m208349200
PubMed ID12393905
Web address (URL)http://europepmc.org/abstract/med/12393905
Publication dates
Published21 Oct 2002

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