Iris Pribilla

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Purified preparations of the inhibitory glycine receptor (GlyR) contain alpha and beta subunits, which share homologous primary structures and a common transmembrane topology with other members of the ligand-gated ion channel superfamily. Here, a beta subunit-specific antiserum was shown to precipitate the [3H]strychnine binding sites localized on alpha(More)
A 93 kd polypeptide associated with the mammalian inhibitory glycine receptor (GlyR) is localized at central synapses and binds with high affinity to polymerized tubulin. This protein, named gephyrin (from the Greek gamma epsilon phi upsilon rho alpha, bridge), is thought to anchor the GlyR to subsynaptic microtubules. Here we report its primary structure(More)
The inhibitory glycine receptor (GlyR) mediates post-synaptic inhibition in spinal cord and other regions of the CNS. Purified mammalian GlyR contains two membrane-spanning subunits 48 kd (alpha) and 58 kd (beta) plus a 93 kd receptor-associated cytoplasmic protein. Here, the primary structure of the beta subunit was deduced from cDNAs isolated from rat(More)
The inhibitory glycine receptor (GlyR) is a ligand-gated chloride channel protein, whose ligand binding alpha subunit occurs in several isoforms in the mammalian central nervous system. Here we show that coexpression of the GlyR-associated protein gephyrin changes the agonist and antagonist binding affinities of GlyRs generated by alpha 2 subunit expression(More)
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