Surface expression of GluR-D AMPA receptor is dependent on an interaction between its C-terminal domain and a 4.1 protein.

Coleman, SK.., Cai, C., Mottershead, D.G., Haapalahti, J.P. and Keinänen, K. 2003. Surface expression of GluR-D AMPA receptor is dependent on an interaction between its C-terminal domain and a 4.1 protein. Journal of Neuroscience. 23 (3), pp. 798-806. https://doi.org/10.1523/jneurosci.23-03-00798.2003

TitleSurface expression of GluR-D AMPA receptor is dependent on an interaction between its C-terminal domain and a 4.1 protein.
TypeJournal article
AuthorsColeman, SK.., Cai, C., Mottershead, D.G., Haapalahti, J.P. and Keinänen, K.
Abstract

Dynamic regulation of the number and activity of AMPA receptors is believed to underlie many forms of synaptic plasticity and is presumably mediated by specific protein-protein interactions involving the C-terminal domain of the receptor. Several proteins interacting with the C-terminal tails of the glutamate receptor (GluR)-A and GluR-B subunits have been identified and implicated in the regulation of endocytosis and exocytosis, clustering, and anchoring of AMPA receptors to the cytoskeleton. In contrast, little is known of the molecular interactions of the GluR-D subunit, or of the mechanisms regulating the traffic of GluR-D-containing AMPA receptors. We analyzed the subcellular localization of homomeric GluR-D receptors carrying C-terminal deletions in transfected human embryonic kidney (HEK) 293 cells and in primary neurons by immunofluorescence microscopy and ELISA. A minimal requirement for a 14-residue cytoplasmic segment for the surface expression of homomeric GluR-D receptors was identified. Previously, a similar region in the GluR-A subunit was implicated in an interaction with 4.1 family proteins. Coimmunoprecipitation demonstrated that GluR-D associated with 4.1 protein(s) in both HEK293 cells and rat brain. Moreover, glutathione S-transferase pull-down experiments showed that the same 14-residue segment is critical for 4.1 binding to GluR-A and GluR-D. Point mutations within this segment dramatically decreased the surface expression of GluR-D in HEK293 cells, with a concomitant loss of the 4.1 interaction. Our findings demonstrate a novel molecular interaction for the GluR-D subunit and suggest that the association with the 4.1 family protein(s) plays an essential role in the transport to and stabilization of GluR-D-containing AMPA receptors at the cell surface.

JournalJournal of Neuroscience
Journal citation23 (3), pp. 798-806
ISSN1529-2401
0270-6474
Year2003
PublisherSociety for Neuroscience
Digital Object Identifier (DOI)https://doi.org/10.1523/jneurosci.23-03-00798.2003
PubMed ID12574408
Web address (URL)http://europepmc.org/abstract/med/12574408
Publication dates
Published01 Feb 2003

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