Investigates how structural mechanics define potassium channel gating, suggesting important regulatory mechanisms.
Potassium (K + ) channels vary in shape and size. Commonly, they form a functional pore through the membrane as an assembly of four subunits. For the predominant family of K + channels at the plant plasma membrane, each subunit comprises a polypeptide of six transmembrane helices with a canonical voltage-sensor domain fused to a pair of pore-lining helices. These constructs give rise to a wide range of behaviours that are nonetheless ‘hard-wired' within the channel protein structure. With cryo-EM data now available for four arabidopsis ( Arabidopsis thaliana ) K + channels, it nonetheless remains an enigma how the structural mechanics give rise to channels that open—or gate—for K + flux across widely differing voltages and how ligands, especially K + itself, regulate this flux.
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Nguyen et al. (2026) studied this question.
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