Key result
Review details Hv1 proton channel structure and gating relationships with voltage-sensing domains.
Why the study?
The structural organization and gating mechanism of Hv1 proton channels remain unclear due to the absence of a pore domain found in other voltage-gated ion channels.
This review summarizes the structural organization and gating mechanisms of the Hv1 proton channel, which lacks a traditional pore domain.
Clarifies Hv1's non-canonical gating; leaves open its relevance to cardiovascular ion channelopathies.
Voltage-gated proton channels have been described in different cells and organisms since the early '80s, but the first member of the family, Hv1, was cloned only recently. The Hv1 channel was found to contain a voltage-sensing domain (VSD), similar to those of voltage-gated sodium, potassium and calcium channels. All these other channels also contain a pore domain, which forms a central pore at the interface of the four subunits. The pore domain is missing in Hv1. This raised several questions on the location of the proton pore and on the mechanism of gating. Here, we briefly review our effort to understand the structural organization of Hv1 channels and discuss the relationship between the gating of Hv1 and the gating of ion-conducting pores recently discovered in the VSDs of mutant voltage-gated potassium and sodium channels.
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Tombola et al. (2009) conducted a review in Hv1 proton channels. This review discusses the structural organization of Hv1 proton channels and the relationship between their gating and that of ion-conducting pores in voltage-sensing domains.
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