Relative positioning of Kv11.1 (hERG) K⁺ channel cytoplasmic domain-located fluorescent tags toward the plasma membrane.

ABSTRACT: Recent cryo-EM data have provided a view of the KCNH potassium channels molecular structures. However, some details about the cytoplasmic domains organization and specially their rearrangements associated to channel functionality are still lacking. Here we used the voltage-dependent dipicrylamine (DPA)-induced quench of fluorescent proteins (FPS) linked to different positions at the cytoplasmic domains of KCNH2 (hERG) to gain some insights about the coarse structure of these channel parts. Fast voltage-clamp fluorometry with HEK293 cells expressing membrane-anchored FPs under conditions in which only the plasma membrane potential is modified, demonstrated DPA voltage-dependent translocation and subsequent FRET-triggered FP quenching. Our data demonstrate for the first time that the distanc

SUBMITTER: Barros F 

PROVIDER: S-EPMC6195548 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature