Assembly and cell surface expression of homomeric and heteromeric 5-HT3 receptors: the role of oligomerisation and chaperone proteins

Gary W. Boyd, Pamela Low, James I. Dunlop, Laura A. Robertson, Audrey Vardy, Jeremy J. Lambert, John A. Peters, Christopher N. Connolly

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63 Citations (Scopus)

Abstract

The ability of differing subunit combinations of 5-HT3 receptors to form functional cell surface receptors was analyzed by a variety of approaches. The results revealed that 5-HT3 receptor assembly occurred within the endoplasmic reticulum (ER) and involved the interaction with chaperone proteins. The 5-HT3A subunit could assemble into functional homomeric receptors that were expressed on the cell surface. In contrast, the 5-HT3B subunit did not exhibit 5-hydroxytryptamine binding or function, could not assemble, and was efficiently retained and degraded within the ER. However, upon the coexpression of the 5-HT3A subunit, 5-HT3B could be “rescued” from the ER and transported to the cell surface to form functional heteromeric receptors with distinct functional characteristics. In support of the existence of homomeric 5-HT3 receptors in vivo, recombinantly expressed 5-HT3A receptors were capable of clustered cell surface expression in cortical neurons.
Original languageEnglish
Pages (from-to)38-50
Number of pages13
JournalMolecular and Cellular Neuroscience
Volume21
Issue number1
DOIs
Publication statusPublished - 2002
Externally publishedYes

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