Functional control of heteromeric Kv2.1/6.4 channels by the voltage sensor domain of the silent Kv6.4 subunit.

ABSTRACT: In the activation process of Kv channels, the S4 segment of the voltage-sensing domain (VSD) moves in the outward direction. A conserved phenylalanine in the transmembrane S2 helix of the VSD is viewed as operating as a charge transfer centre (CTC) that interacts with a positively charged arginine of the S4 helix. This phenylalanine is highly sensitive to diverse substitutions. Kv2.1 subunits can form functional homotetrameric channels on their own whereas 'silent' Kv6.4 subunits can only contribute to functional heterotetrameric channels. We used concatenated dimers of Kv2.1 and Kv6.4 subunits to define the stoichiometry and position of these subunits in functional heterotetrameric channels. Our results demonstrate that mutating the phenylalanine F273 of the Kv6.4 subunits in Kv 2.1_6.4 c

SUBMITTER: Tewari D 

PROVIDER: S-EPMC12206438 | biostudies-literature | 2025 Jun

REPOSITORIES: biostudies-literature