Stability of ligand-binding domain dimer assembly controls kainate receptor desensitization.

ABSTRACT: AMPA and kainate receptors mediate fast synaptic transmission. AMPA receptor ligand-binding domains form dimers, which are key functional units controlling ion-channel activation and desensitization. Dimer stability is inversely related to the rate and extent of desensitization. Kainate and AMPA receptors share common structural elements, but functional measurements suggest that subunit assembly and gating differs between these subtypes. To investigate this, we constructed a library of GluR6 kainate receptor mutants and directly measured changes in kainate receptor dimer stability by analytical ultracentrifugation, which, combined with electrophysiological experiments, revealed an inverse correlation between dimer stability and the rate of desensitization. We solved crystal structures for

SUBMITTER: Chaudhry C 

PROVIDER: S-EPMC2688536 | biostudies-literature | 2009 May

REPOSITORIES: biostudies-literature