Elucidating the Structural Basis of the Intracellular pH Sensing Mechanism of TASK-2 K₂P Channels.

ABSTRACT: Two-pore domain potassium (K₂P) channels maintain the cell's background conductance by stabilizing the resting membrane potential. They assemble as dimers possessing four transmembrane helices in each subunit. K₂P channels were crystallized in "up" and "down" states. The movements of the pore-lining transmembrane TM4 helix produce the aperture or closure of side fenestrations that connect the lipid membrane with the central cavity. When the TM4 helix is in the up-state, the fenestrations are closed, while they are open in the down-state. It is thought that the fenestration states are related to the activity of K₂P channels and the opening of the channels preferentially occurs from the up-state. TASK-2, a member of the TALK subfamily of K₂P channe

SUBMITTER: Bustos D 

PROVIDER: S-EPMC7013731 | biostudies-literature | 2020 Jan

REPOSITORIES: biostudies-literature