Protein interactions involving the gamma2 large cytoplasmic loop of GABA(A) receptors modulate conductance.

ABSTRACT: Native GABA(A) channels display a single-channel conductance ranging between approximately 10 and 90 pS. Diazepam increases the conductance of some of these native channels but never those of recombinant receptors, unless they are coexpressed with GABARAP. This trafficking protein clusters recombinant receptors in the membrane, suggesting that high-conductance channels arise from receptors that are at locally high concentrations. The amphipathic (MA) helix that is present in the large cytoplasmic loop of every subunit of all ligand-gated ion channels mediates protein-protein interactions. Here we report that when applied to inside-out patches, a peptide mimicking the MA helix of the gamma2 subunit (gamma(381-403)) of the GABA(A) receptor abrogates the potentiating effect of diazepam on bot

SUBMITTER: Everitt AB 

PROVIDER: S-EPMC2812045 | biostudies-literature | 2009 Dec

REPOSITORIES: biostudies-literature