Trafficking of 5-HT3 and GABA(A) receptors (Review)

    Research output: Contribution to journalReview article

    17 Citations (Scopus)

    Abstract

    The 5-HT3 and GABA(A) receptors are members of the Cys-loop family of neurotransmitter-gated ion channels that also include receptors for glycine and acetylcholine. The 5-HT3 and acetylcholine receptors (cationic ion channels) and the GABA(A) and glycine receptors (anionic ion channels) generally depolarize or hyperpolarize, respectively, the neuronal membrane. Within the amino-terminal extracellular region, all members of this family exhibit a similar architecture of ligand binding domains and a number of key residues are completely conserved. The molecular characterization of their ligand binding and gating characteristics has benefited from the existence of a large repertoire of individual subunits that contribute to the pentameric ion channel. Although differences do exist, advances in our knowledge of one member offers valuable insight into the family as a whole. Each member of the Cys-loop receptors (and all other multimeric ion channels) must face the same challenges: How to assemble individual subunits into an ion channel and which subunits to use? How are assembled receptors distinguished from those that are unassembled or misassembled, then exported from the endoplasmic reticulum and delivered to the cell surface? How are they targeted to, and anchored at synaptic and extrasynaptic sites? How and when are they to be removed from these sites to provide long-term regulation of neuronal activity? In this review, we summarize our current knowledge for the 5-HT3 and GABA(A) receptors that have provided complementary information and helped us build an overall picture of how receptor biogenesis and trafficking occurs.

    Original languageEnglish
    Pages (from-to)293-301
    Number of pages9
    JournalMolecular Membrane Biology
    Volume25
    Issue number4
    DOIs
    Publication statusPublished - 2008

    Keywords

    • ER export
    • trafficking
    • synaptic localization
    • endocytosis
    • neurotransmitter
    • receptor
    • membrane biogenesis
    • targeting
    • CELL-SURFACE EXPRESSION
    • 5-HYDROXYTRYPTAMINE TYPE-3 RECEPTORS
    • INHIBITORY SYNAPTIC-TRANSMISSION
    • AP2 ADAPTER COMPLEX
    • PROTEIN-KINASE-C
    • A RECEPTORS
    • SUBCELLULAR-LOCALIZATION
    • FUNCTIONAL EXPRESSION
    • INACTIVE PROTEIN
    • MAMMALIAN-CELLS

    Cite this

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    abstract = "The 5-HT3 and GABA(A) receptors are members of the Cys-loop family of neurotransmitter-gated ion channels that also include receptors for glycine and acetylcholine. The 5-HT3 and acetylcholine receptors (cationic ion channels) and the GABA(A) and glycine receptors (anionic ion channels) generally depolarize or hyperpolarize, respectively, the neuronal membrane. Within the amino-terminal extracellular region, all members of this family exhibit a similar architecture of ligand binding domains and a number of key residues are completely conserved. The molecular characterization of their ligand binding and gating characteristics has benefited from the existence of a large repertoire of individual subunits that contribute to the pentameric ion channel. Although differences do exist, advances in our knowledge of one member offers valuable insight into the family as a whole. Each member of the Cys-loop receptors (and all other multimeric ion channels) must face the same challenges: How to assemble individual subunits into an ion channel and which subunits to use? How are assembled receptors distinguished from those that are unassembled or misassembled, then exported from the endoplasmic reticulum and delivered to the cell surface? How are they targeted to, and anchored at synaptic and extrasynaptic sites? How and when are they to be removed from these sites to provide long-term regulation of neuronal activity? In this review, we summarize our current knowledge for the 5-HT3 and GABA(A) receptors that have provided complementary information and helped us build an overall picture of how receptor biogenesis and trafficking occurs.",
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    Trafficking of 5-HT3 and GABA(A) receptors (Review). / Connolly, Christopher.

    In: Molecular Membrane Biology, Vol. 25, No. 4, 2008, p. 293-301.

    Research output: Contribution to journalReview article

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    T1 - Trafficking of 5-HT3 and GABA(A) receptors (Review)

    AU - Connolly, Christopher

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    N2 - The 5-HT3 and GABA(A) receptors are members of the Cys-loop family of neurotransmitter-gated ion channels that also include receptors for glycine and acetylcholine. The 5-HT3 and acetylcholine receptors (cationic ion channels) and the GABA(A) and glycine receptors (anionic ion channels) generally depolarize or hyperpolarize, respectively, the neuronal membrane. Within the amino-terminal extracellular region, all members of this family exhibit a similar architecture of ligand binding domains and a number of key residues are completely conserved. The molecular characterization of their ligand binding and gating characteristics has benefited from the existence of a large repertoire of individual subunits that contribute to the pentameric ion channel. Although differences do exist, advances in our knowledge of one member offers valuable insight into the family as a whole. Each member of the Cys-loop receptors (and all other multimeric ion channels) must face the same challenges: How to assemble individual subunits into an ion channel and which subunits to use? How are assembled receptors distinguished from those that are unassembled or misassembled, then exported from the endoplasmic reticulum and delivered to the cell surface? How are they targeted to, and anchored at synaptic and extrasynaptic sites? How and when are they to be removed from these sites to provide long-term regulation of neuronal activity? In this review, we summarize our current knowledge for the 5-HT3 and GABA(A) receptors that have provided complementary information and helped us build an overall picture of how receptor biogenesis and trafficking occurs.

    AB - The 5-HT3 and GABA(A) receptors are members of the Cys-loop family of neurotransmitter-gated ion channels that also include receptors for glycine and acetylcholine. The 5-HT3 and acetylcholine receptors (cationic ion channels) and the GABA(A) and glycine receptors (anionic ion channels) generally depolarize or hyperpolarize, respectively, the neuronal membrane. Within the amino-terminal extracellular region, all members of this family exhibit a similar architecture of ligand binding domains and a number of key residues are completely conserved. The molecular characterization of their ligand binding and gating characteristics has benefited from the existence of a large repertoire of individual subunits that contribute to the pentameric ion channel. Although differences do exist, advances in our knowledge of one member offers valuable insight into the family as a whole. Each member of the Cys-loop receptors (and all other multimeric ion channels) must face the same challenges: How to assemble individual subunits into an ion channel and which subunits to use? How are assembled receptors distinguished from those that are unassembled or misassembled, then exported from the endoplasmic reticulum and delivered to the cell surface? How are they targeted to, and anchored at synaptic and extrasynaptic sites? How and when are they to be removed from these sites to provide long-term regulation of neuronal activity? In this review, we summarize our current knowledge for the 5-HT3 and GABA(A) receptors that have provided complementary information and helped us build an overall picture of how receptor biogenesis and trafficking occurs.

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    KW - membrane biogenesis

    KW - targeting

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    KW - 5-HYDROXYTRYPTAMINE TYPE-3 RECEPTORS

    KW - INHIBITORY SYNAPTIC-TRANSMISSION

    KW - AP2 ADAPTER COMPLEX

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    U2 - 10.1080/09687680801898503

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    JF - Molecular Membrane Biology

    SN - 0968-7688

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