Ontology highlight
ABSTRACT:
SUBMITTER: Ben Soussia I
PROVIDER: S-EPMC6377628 | biostudies-literature | 2019 Feb
REPOSITORIES: biostudies-literature
Nature communications 20190215 1
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 ...[more]