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• W2025249969 abstract "The strychnine-sensitive glycine receptor (GlyR) is a ligand-gated ion channel that mediates fast synaptic inhibition in the vertebrate central nervous system. As a member of the family of Cys-loop receptors, it assembles from five homologous subunits (GlyRα1–4 and -β). Each subunit contains an extracellular ligand binding domain, four transmembrane domains (TM), and an intracellular domain, formed by the loop connecting TM3 and TM4 (TM3–4 loop). The TM3–4 loops of the subunits GlyRα1 and -α3 harbor a conserved basic motif, which is part of a potential nuclear localization signal. When tested for functionality by live cell imaging of green fluorescent protein and β-galactosidase-tagged domain constructs, the TM3–4 loops of GlyRα1 and -α3, but not of GlyRα2 and -β, exhibited nuclear sorting activity. Subunit specificity may be attributed to slight amino acid alterations in the basic motif. In yeast two-hybrid screening and GST pulldown assays, karyopherin α3 and α4 were found to interact with the TM3–4 loop, providing a molecular mechanism for the observed intracellular trafficking. These results indicate that the multifunctional basic motif of the TM3–4 loop is capable of mediating a karyopherin-dependent intracellular sorting of full-length GlyRs. The strychnine-sensitive glycine receptor (GlyR) is a ligand-gated ion channel that mediates fast synaptic inhibition in the vertebrate central nervous system. As a member of the family of Cys-loop receptors, it assembles from five homologous subunits (GlyRα1–4 and -β). Each subunit contains an extracellular ligand binding domain, four transmembrane domains (TM), and an intracellular domain, formed by the loop connecting TM3 and TM4 (TM3–4 loop). The TM3–4 loops of the subunits GlyRα1 and -α3 harbor a conserved basic motif, which is part of a potential nuclear localization signal. When tested for functionality by live cell imaging of green fluorescent protein and β-galactosidase-tagged domain constructs, the TM3–4 loops of GlyRα1 and -α3, but not of GlyRα2 and -β, exhibited nuclear sorting activity. Subunit specificity may be attributed to slight amino acid alterations in the basic motif. In yeast two-hybrid screening and GST pulldown assays, karyopherin α3 and α4 were found to interact with the TM3–4 loop, providing a molecular mechanism for the observed intracellular trafficking. These results indicate that the multifunctional basic motif of the TM3–4 loop is capable of mediating a karyopherin-dependent intracellular sorting of full-length GlyRs." @default.
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• W2025249969 date "2010-02-01" @default.
• W2025249969 modified "2023-10-17" @default.
• W2025249969 title "Multifunctional Basic Motif in the Glycine Receptor Intracellular Domain Induces Subunit-specific Sorting" @default.
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• W2025249969 doi "https://doi.org/10.1074/jbc.m109.030460" @default.
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