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Wobig, L.* ; Wolfenstetter, T.* ; Fechner, S.* ; Bönigk, W.* ; Körschen, H.G.* ; Jikeli, J.F.* ; Trötschel, C.* ; Feederle, R. ; Kaupp, U.B.* ; Seifert, R.* ; Berger, T.K.*

A family of hyperpolarization-activated channels selective for.

Proc. Natl. Acad. Sci. U.S.A. 117, 13783-13791 (2020)
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Proton (H + ) channels are special: They select protons against other ions that are up to a millionfold more abundant. Only a few pro- ton channels have been identified so far. Here, we identify a fam- ily of voltage -gated ?pacemaker ? channels, HCNL1, that are exquisitely selective for protons. HCNL1 activates during hyperpo- larization and conducts protons into the cytosol. Surprisingly, pro- tons permeate through the channel ?s voltage -sensing domain, whereas the pore domain is nonfunctional. Key to proton perme- ation is a methionine residue that interrupts the series of regularly spaced arginine residues in the S4 voltage sensor. HCNL1 forms a tetramer and thus contains four proton pores. Unlike classic HCN channels, HCNL1 is not gated by cyclic nucleotides. The channel is present in zebrafish sperm and carries a proton inward current that acidifies the cytosol. Our results suggest that protons rather than cyclic nucleotides serve as cellular messengers in zebrafish sperm. Through small modifications in two key functional do- mains, HCNL1 evolutionarily adapted to a low-Na + freshwater en- vironment to conserve sperm ?s ability to depolarize.
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Publication type Article: Journal article
Document type Scientific Article
Keywords Hcnl1 Channel ; Proton Channel ; Voltage-sensing Domain ; Hcn Channel; Controls Chemosensation; Transient Protonation; Conserved Aspartate; Pacemaker Channels; Ion-channel; Hv1; Pore; Currents; Identification; Domain
Language english
Publication Year 2020
HGF-reported in Year 2020
ISSN (print) / ISBN 0027-8424
e-ISSN 1091-6490
Journal Proceedings of the National Academy of Sciences of the United States of America
Quellenangaben Volume: 117, Issue: 24, Pages: 13783-13791 Article Number: , Supplement: ,
Publisher National Academy of Sciences
Publishing Place 2101 Constitution Ave Nw, Washington, Dc 20418 Usa
Reviewing status Peer reviewed
Institute(s) CF Monoclonal Antibodies (CF-MAB)
POF-Topic(s) 30201 - Metabolic Health
Research field(s) Helmholtz Diabetes Center
PSP Element(s) G-502210-001
DOI 10.1073/pnas.2001214117
WOS ID WOS:000546043800003
Scopus ID 85086682243
PubMed ID 32467169
Erfassungsdatum 2020-06-03
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