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Cited by 333

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Assembly and Cell Surface Expression of Heteromeric and Homomeric γ-Aminobutyric Acid Type A Receptors

Open access
Connolly, Christopher N., Krishek, Belinda J., McDonald, Bernard J., Smart, Trevor G., Moss, Stephen J.·1996·Journal of Biological Chemistry

Abstract

The ability of differing subunit combinations of gamma-aminobutyric acid type A (GABAA) receptors produced from murine alpha 1, beta 2, and gamma 2L subunits to form functional cell surface receptors was analyzed in both A293 cells and Xenopus oocytes using a combination of molecular, electrophysiological, biochemical, and morphological approaches. The results revealed that GABAA receptor assembly occurred within the endoplasmic reticulum and involved the interaction with the chaperone molecules immunoglobulin heavy chain binding protein and calnexin. Despite all three subunits possessing the ability to oligomerize with each other, only alpha 1 beta 2 and alpha 1 beta 2 gamma 2L subunit combinations could produce functional surface expression in a process that was not dependent on N-linked glycosylation. Single subunits and the alpha 1 gamma 2L and beta 2 gamma 2L combinations were retained within the endoplasmic reticulum. These results suggest that receptor assembly occurs by defined pathways, which may serve to limit the diversity of GABAA receptors that exist on the surface of neurons.

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Metadata

Authors
Connolly, C. N., Krishek, B. J., McDonald, B. J., Smart, T. G., & Moss, S. J.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1996-01
Volume
271
Issue
1
Pages
89-96
ISSN
0021-9258 (ISSN-L)
OpenAlex
W1973238622
Cited by
333
References
1
FWCI
7.00
Type
journal article
Language
en
Open access
hybrid

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Connolly, C. N., Krishek, B. J., McDonald, B. J., Smart, T. G., & Moss, S. J. (1996). Assembly and Cell Surface Expression of Heteromeric and Homomeric γ-Aminobutyric Acid Type A Receptors. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.271.1.89

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