Interface interactions modulating desensitization of the kainate-selective ionotropic glutamate receptor subunit GluR6.

ABSTRACT: Ionotropic glutamate receptors from the AMPA and kainate subfamilies share many functional and structural features, but it is unclear whether this similarity extends to the molecular mechanisms underlying receptor desensitization. The current model for desensitization in AMPA receptors involves the rearrangement of dimers formed between subunit agonist binding domains. Key evidence for this has come from a single point mutant (from leucine to tyrosine) that abolished desensitization and that was shown to stabilize the binding domain dimer. However, the desensitization of kainate receptors appears to differ from that of AMPA receptors in several key respects. Although the kinetics of AMPA receptor gating and desensitization are consistent with channels formed from two dimers, similar eviden

SUBMITTER: Zhang Y 

PROVIDER: S-EPMC6674465 | biostudies-literature | 2006 Sep

REPOSITORIES: biostudies-literature