title: Philosophy of voltage-gated proton channels.
abstract: In this review, voltage-gated proton channels are considered from a mainly teleological perspective. Why do proton channels exist? What good are they? Why did they go to such lengths to develop several unique hallmark properties such as extreme selectivity and ΔpH-dependent gating? Why is their current so minuscule? How do they manage to be so selective? What is the basis for our belief that they conduct H(+) and not OH(-)? Why do they exist in many species as dimers when the monomeric form seems to work quite well? It is hoped that pondering these questions will provide an introduction to these channels and a way to logically organize their peculiar properties as well as to understand how they are able to carry out some of their better-established biological functions.
authors.affiliation: Department of Molecular Biophysics and Physiology, Rush University, , 1750 West Harrison, Chicago, IL 60612, USA.
authors.forename: Thomas E
authors.initials: TE
authors.lastname: DeCoursey
authors.forename: Jonathan
authors.initials: J
authors.lastname: Hosler
mesh_terms: D020346:Aquaporins / Q000378:metabolism*; D019281:Dimerization; D004553:Electric Conductivity; D006801:Humans; D007473:Ion Channels / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D008958:Models, Molecular; D010802:Phylogeny; D018892:Proton-Motive Force / Q000502:physiology; D016897:Respiratory Burst / Q000502:physiology*; D013045:Species Specificity; D014763:Viral Matrix Proteins / Q000378:metabolism*; D000086082:Viroporin Proteins
chemical_list: D020346:Aquaporins; D007473:Ion Channels; D014763:Viral Matrix Proteins; C510235:HVCN1 protein, human; C488937:M2 protein, Influenza A virus; D000086082:Viroporin Proteins
keywords: HV1; HVCN1; ion channels; permeation; selectivity; voltage sensing