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

TY - JOUR

T1 - Assembly and cell surface expression of homomeric and heteromeric 5-HT3 receptors

T2 - the role of oligomerization and chaperone proteins

AU - Boyd, Gary W.

AU - Low, Pamela

AU - Dunlop, James I.

AU - Robertson, Laura A.

AU - Vardy, Audrey

AU - Lambert, Jeremy J.

AU - Peters, John A.

AU - Connolly, Christopher N.

N1 - dc.publisher: Elsevier

PY - 2002

Y1 - 2002

N2 - 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.

AB - 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.

U2 - 10.1006/mcne.2002.1160

DO - 10.1006/mcne.2002.1160

M3 - Article

SN - 1044-7431

VL - 21

SP - 38

EP - 50

JO - Molecular and Cellular Neuroscience

JF - Molecular and Cellular Neuroscience

IS - 1

ER -