Cell surface expression of 5-hydroxytryptamine type 3 receptors is promoted by RIC-3

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

    Research output: Contribution to journalArticle

    51 Citations (Scopus)

    Abstract

    RIC-3 has been identified as a molecule essential for the recruitment of functional nicotinic acetylcholine receptors composed of a7, but it exhibits inhibitory effects on a4b2 or a3b4 receptors. In this study, we investigated the role of RIC-3 in the recruitment of 5-hydroxytryptamine type 3A (5-HT3A3A3A) receptors to the cell surface. Although RIC-3 is not essential for the surface transport of 5-HT3A 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. RIC-3 and 5-HT (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)(, suggests that RIC)(-3)(-3) (may play a role in 5-HT)(3A) receptor folding, assembly, or transport to the cell surface.

    Original languageEnglish
    Pages (from-to)22502-22507
    Number of pages6
    JournalJournal of Biological Chemistry
    Volume280
    Issue number23
    DOIs
    Publication statusPublished - 10 Jun 2005

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    Receptors, Serotonin, 5-HT3
    Serotonin
    Endoplasmic Reticulum
    Serotonin Receptors
    Nicotinic Receptors
    Cell Surface Receptors
    Molecules
    Carrier Proteins

    Cite this

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    title = "Cell surface expression of 5-hydroxytryptamine type 3 receptors is promoted by RIC-3",
    abstract = "RIC-3 has been identified as a molecule essential for the recruitment of functional nicotinic acetylcholine receptors composed of a7, but it exhibits inhibitory effects on a4b2 or a3b4 receptors. In this study, we investigated the role of RIC-3 in the recruitment of 5-hydroxytryptamine type 3A (5-HT3A3A3A) receptors to the cell surface. Although RIC-3 is not essential for the surface transport of 5-HT3A 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. RIC-3 and 5-HT (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)(, suggests that RIC)(-3)(-3) (may play a role in 5-HT)(3A) receptor folding, assembly, or transport to the cell surface.",
    author = "Aixin Cheng and McDonald, {Neil A.} and Connolly, {Christopher N.}",
    year = "2005",
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    language = "English",
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    Cell surface expression of 5-hydroxytryptamine type 3 receptors is promoted by RIC-3. / Cheng, Aixin; McDonald, Neil A.; Connolly, Christopher N.

    In: Journal of Biological Chemistry, Vol. 280, No. 23, 10.06.2005, p. 22502-22507.

    Research output: Contribution to journalArticle

    TY - JOUR

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    AU - Cheng, Aixin

    AU - McDonald, Neil A.

    AU - Connolly, Christopher N.

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    N2 - RIC-3 has been identified as a molecule essential for the recruitment of functional nicotinic acetylcholine receptors composed of a7, but it exhibits inhibitory effects on a4b2 or a3b4 receptors. In this study, we investigated the role of RIC-3 in the recruitment of 5-hydroxytryptamine type 3A (5-HT3A3A3A) receptors to the cell surface. Although RIC-3 is not essential for the surface transport of 5-HT3A 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. RIC-3 and 5-HT (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)(, suggests that RIC)(-3)(-3) (may play a role in 5-HT)(3A) receptor folding, assembly, or transport to the cell surface.

    AB - RIC-3 has been identified as a molecule essential for the recruitment of functional nicotinic acetylcholine receptors composed of a7, but it exhibits inhibitory effects on a4b2 or a3b4 receptors. In this study, we investigated the role of RIC-3 in the recruitment of 5-hydroxytryptamine type 3A (5-HT3A3A3A) receptors to the cell surface. Although RIC-3 is not essential for the surface transport of 5-HT3A 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. RIC-3 and 5-HT (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)(, suggests that RIC)(-3)(-3) (may play a role in 5-HT)(3A) receptor folding, assembly, or transport to the cell surface.

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