Mutation of a single residue promotes gating of vertebrate and invertebrate two-pore domain potassium channels.
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ABSTRACT:
SUBMITTER: Ben Soussia I
PROVIDER: S-EPMC6377628 | biostudies-literature | 2019 Feb
REPOSITORIES: biostudies-literature
Publications
Mutation of a single residue promotes gating of vertebrate and invertebrate two-pore domain potassium channels.
Ben Soussia Ismail I El Mouridi Sonia S Kang Dawon D Leclercq-Blondel Alice A Khoubza Lamyaa L Tardy Philippe P Zariohi Nora N Gendrel Marie M Lesage Florian F Kim Eun-Jin EJ Bichet Delphine D Andrini Olga O Boulin Thomas T
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]
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