Voltage-sensor gating charge interactions bimodally regulate voltage dependence and kinetics of calcium channel activation.

ABSTRACT: Voltage-sensing domains (VSDs) are highly conserved protein modules that regulate the activation of voltage-gated ion channels. In response to membrane depolarization, positive gating charges in the S4 helix of VSDs move across the membrane electric field, which is focused at the hydrophobic constriction site (HCS) in the center of the VSD. This conformational change is translated into opening of the channel gate. Transient interactions of the gating charges with negatively charged countercharges in the adjacent helices are critical for catalyzing this state transition and for determining its voltage dependence and kinetics. However, the mechanism by which the sequential interactions between the multiple gating- and countercharges regulate these properties remains poorly understood. Here,

SUBMITTER: Heiss MC 

PROVIDER: S-EPMC7618026 | biostudies-literature | 2025 Sep

REPOSITORIES: biostudies-literature