Molecular architecture of the Gα_i-bound TRPC5 ion channel.

ABSTRACT: G-protein coupled receptors (GPCRs) and ion channels serve as key molecular switches through which extracellular stimuli are transformed into intracellular effects, and it has long been postulated that ion channels are direct effector molecules of the alpha subunit of G-proteins (Gα). However, no complete structural evidence supporting the direct interaction between Gα and ion channels is available. Here, we present the cryo-electron microscopy structures of the human transient receptor potential canonical 5 (TRPC5)-Gα_i3 complexes with a 4:4 stoichiometry in lipid nanodiscs. Remarkably, Gα_i3 binds to the ankyrin repeat edge of TRPC5 ~ 50 Å away from the cell membrane. Electrophysiological analysis shows that Gα_i3 increases the sensitivity of TRPC5 to phosph

SUBMITTER: Won J 

PROVIDER: S-EPMC10156788 | biostudies-literature | 2023 May

REPOSITORIES: biostudies-literature