Mutation of a single residue promotes gating of vertebrate and invertebrate two-pore domain potassium channels.

ABSTRACT: Mutations that modulate the activity of ion channels are essential tools to understand the biophysical determinants that control their gating. Here, we reveal the conserved role played by a single amino acid position (TM2.6) located in the second transmembrane domain of two-pore domain potassium (K2P) channels. Mutations of TM2.6 to aspartate or asparagine increase channel activity for all vertebrate K2P channels. Using two-electrode voltage-clamp and single-channel recording techniques, we find that mutation of TM2.6 promotes channel gating via the selectivity filter gate and increases single channel open probability. Furthermore, channel gating can be progressively tuned by using different amino acid substitutions. Finally, we show that the role of TM2.6 was conserved during evolution by

SUBMITTER: Ben Soussia I 

PROVIDER: S-EPMC6377628 | biostudies-literature | 2019 Feb

REPOSITORIES: biostudies-literature