Coexpression of the receptor-associated protein gephyrin changes the ligand binding affinities of alpha 2 glycine receptors.
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 in 293 kidney cells. Thus, a receptor-associated protein modifies the functional properties of a neurotransmitter receptor. This may contribute to an optimization of the postsynaptic neurotransmitter response.
Takagi
T
T
Zentrum für Molekulare Biologie, Universität Heidelberg, Germany.
Pribilla
I
I
Kirsch
J
J
Betz
H
H
D000818:Animals; D002352:Carrier Proteins / Q000235:genetics / Q000378:metabolism*; D002460:Cell Line; D015870:Gene Expression; D005998:Glycine / Q000378:metabolism*; D006801:Humans; D008024:Ligands; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism*; D051381:Rats; D018009:Receptors, Glycine; D017981:Receptors, Neurotransmitter / Q000378:metabolism*; D013331:Strychnine / Q000494:pharmacology
D002352:Carrier Proteins; D008024:Ligands; D008565:Membrane Proteins; D018009:Receptors, Glycine; D017981:Receptors, Neurotransmitter; C073441:gephyrin; D013331:Strychnine; D005998:Glycine