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J. Biol. Chem., Vol. 280, Issue 23, 22502-22507, June 10, 2005

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Cell Surface Expression of 5-Hydroxytryptamine Type 3 Receptors Is Promoted by RIC-3^*

Aixin Cheng, Neil A. McDonald, and Christopher N. Connolly

From the Department of Pharmacology & Neuroscience, Ninewells Medical School, University of Dundee, Dundee DD1 9SY, Scotland, United Kingdom

RIC-3 has been identified as a molecule essential for the recruitment of functional nicotinic acetylcholine receptors composed of 7, but it exhibits inhibitory effects on 42 or 34 receptors. In this study, we investigated the role of RIC-3 in the recruitment of 5-hydroxytryptamine type 3A (5-HT_3A) receptors to the cell surface. Although RIC-3 is not essential for the surface transport of 5-HT_3A receptors, we found that its presence enhances both receptor transport and function in a concentration-dependent manner. RIC-3 is localized to the endoplasmic reticulum, as evidenced by co-localization with the chaperone molecule, binding protein (BiP). RIC-3 is not detected at significant levels on the cell surface when expressed alone or in the presence of 5-HT_3A. RIC-3 and 5-HT_3A show a low level interaction that is transient (<4 h). That RIC-3 can interact with an endoplasmic reticulum-retained 5-HT_3A construct, combined with the transient interaction observed and lack of significant surface-expressed RIC-3, suggests that RIC-3 may play a role in 5-HT_3A receptor folding, assembly, or transport to the cell surface.

Received for publication, December 21, 2004 , and in revised form, April 1, 2005.

^* This work was supported by Biotechnology and Biological Sciences Research Council Grant 94/C18896, Tenovus Scotland, and Anonymous Trust. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed. Tel.: 44-3182-632527; Fax: 44-3182-667120; E-mail: c.n.connolly{at}dundee.ac.uk.

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