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Incorporation of a gephyrin‐binding motif targets NMDA receptors to gephyrin‐rich domains in HEK 293 cells
Author(s) -
Kins Stefan,
Kuhse Jochen,
Laube Bodo,
Betz Heinrich,
Kirsch Joachim
Publication year - 1999
Publication title -
european journal of neuroscience
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.346
H-Index - 206
eISSN - 1460-9568
pISSN - 0953-816X
DOI - 10.1046/j.1460-9568.1999.00527.x
Subject(s) - gephyrin , hek 293 cells , microbiology and biotechnology , receptor , scaffold protein , neuroscience , biology , glycine receptor , genetics , signal transduction , amino acid , glycine
The peripheral membrane protein gephyrin is essential for the postsynaptic localization of inhibitory glycine receptors (GlyRs). Binding of gephyrin to the GlyR β subunit is mediated by a sequence motif located in the intracellular loop region connecting transmembrane segments 3 and 4. Here, insertion of this binding motif is shown to alter the subcellular distribution of an excitatory neurotransmitter receptor in transfected mammalian cells. Upon coexpression with gephyrin, a mutant N ‐methyl‐ d ‐aspartate (NMDA) receptor containing NMDA receptor 1 (NR1) subunits which harboured a gephyrin‐binding motif within its cytoplasmic tail region, was targeted to intracellular gephyrin‐rich domains, as previously observed for the GlyR β subunit. Our data indicate that a gephyrin‐binding motif located in a cytoplasmic domain of an integral membrane protein suffices for routing to gephyrin‐rich domains.