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The voltage-gated proton channel, HV1, is notoriously unique among ion channels (1), and plays key roles in the health and disease of diverse tissues and species (2). Li et al. (3) combine biochemical, computational, and electron paramagnetic resonance (EPR) spectroscopic approaches to shed light on structural aspects of the human proton channel, hHV1. Their results advance the field in several key areas, culminating in a bold new model for gating. The voltage-sensing domain (VSD) is the part of voltage-gated ion channels that senses the electrical potential across the cell membrane where the channel resides. Most such channels open upon membrane depolarization, which is accomplished mainly by cationic amino acids located in the fourth transmembrane helical segment (S4) moving outward when the inside of the cell is made more positive. This movement is transduced from the VSD (S1–S4) to the pore region (S5–S6), opening a conduction pathway. In addition to biologically important voltage-gated K+, Na+, Ca2+, and H+ channels, other classes of membrane proteins with VSDs exist that are not channels at all. One example is a voltage-sensing phosphatase (VSP), an enzyme whose activity is regulated by membrane potential. In a landmark study in 2014 (4), the Li–Perozo group reported crystal structures for CiVSP in both “down” and “up” conformations, the first VSD-containing molecule to have structures determined in both states. Voltage-gated ion channels are closed at negative voltages, and open upon depolarization as the S4 helix moves “up” through the membrane electrical field. Because the VSP is not a channel, “closed” and “open” become “down” and “up.” The gene for hHV1 was identified only in 2006 (5). To the astonishment of everyone, the gene product bore a striking resemblance to the VSD of other voltage-gated ion channels, …

Structural revelations of the human proton channel