Structural basis for KCTD-mediated rapid desensitization of GABA_B signalling.

ABSTRACT: The GABA_B (γ-aminobutyric acid type B) receptor is one of the principal inhibitory neurotransmitter receptors in the brain, and it signals through heterotrimeric G proteins to activate a variety of effectors, including G-protein-coupled inwardly rectifying potassium channels (GIRKs)^1,2. GABA_B-receptor signalling is tightly regulated by auxiliary subunits called KCTDs, which control the kinetics of GIRK activation and desensitization^3-5. However, the mechanistic basis for KCTD modulation of GABA_B signalling remains incompletely understood. Here, using a combination of X-ray crystallography, electron microscopy, and functional and biochemical experiments, we reveal the molecular details of KCTD binding to both GABA_B receptors

SUBMITTER: Zheng S 

PROVIDER: S-EPMC6405316 | biostudies-literature | 2019 Mar

REPOSITORIES: biostudies-literature