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Hydrophobic Interactions Mediate Binding of the Glycine Receptor β‐Subunit to Gephyrin
Author(s) -
Kneussel Matthias,
Hermann Achim,
Kirsch Joachim,
Betz Heinrich
Publication year - 1999
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1046/j.1471-4159.1999.0721323.x
Subject(s) - gephyrin , glycine receptor , glycine , protein subunit , chemistry , biophysics , microbiology and biotechnology , neuroscience , biochemistry , biology , amino acid , gene
: Glycine receptors (GlyRs) are ligand‐gated chloride channel proteins composed of α‐ and β‐subunits. GlyRs are located to and anchored at postsynaptic sites by the receptorassociated protein gephyrin. Previous work from our laboratory has identified a core motif for gephyrin binding in the cytoplasmic loop of the GlyR β‐subunit. Here, we localized amino acid residues implicated in gephyrin binding by site‐directed mutagenesis. In a novel transfection assay, a green fluorescent protein‐gephyrin binding motif fusion protein was used to monitor the consequences of amino acid substitutions for β‐subunit interaction with gephyrin. Only multiple, but not single, replacements of hydrophobic side chains abolished the interaction between the two proteins. Our data are consistent with gephyrin binding being mediated by the hydrophobic side of an imperfect amphipathic helix.