Evidence map›Paper›PMID 36752823›Full record

ArticleThe Journal of general physiology2023

Similar voltage-sensor movement in spHCN channels can cause closing, opening, or inactivation.

Xiaoan Wu, Kevin P Cunningham, Rosamary Ramentol, Marta E Perez, H Peter Larsson

Open access · hybridAbstract read
In one paragraph

Article in The Journal of general physiology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
2.0field-weighted citation impact, top 14% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

7 citing papers in PubMed, 13 citations in OpenAlex.

  1. Article
  2. Extracellular salt bridge networks around S4 implicated in HCN channel gating and heart disease.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Xiaoan WuDepartment of Physiology and Biophysics, University of Miami Miller School of Medicine , Miami, FL, USA.ORCID 0000-0003-2098-7298
Kevin P CunninghamDepartment of Physiology and Biophysics, University of Miami Miller School of Medicine , Miami, FL, USA.ORCID 0000-0001-6772-0107
Rosamary RamentolDepartment of Physiology and Biophysics, University of Miami Miller School of Medicine , Miami, FL, USA.
Marta E PerezDepartment of Physiology and Biophysics, University of Miami Miller School of Medicine , Miami, FL, USA.
H Peter LarssonDepartment of Physiology and Biophysics, University of Miami Miller School of Medicine , Miami, FL, USA.ORCID 0000-0002-1688-2525
University of Miami · US

Funding

Modulation of KCNQ1 channel activityR01GM109762 · NIGMS · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI KASS, ROBERT S, LARSSON, HANS PETER · 2014 to 2022
$3.1M
Activation mechanism in HCN channels.R01GM139164 · NIGMS · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI BARRO-SORIA, RENE · 2020 to 2023
$1.5M
NIGMS NIH HHS R01 GM109762NIGMS NIH HHS R01 GM139164NIH HHS R01 GM109762
6 · The paper itself

Abstract

Hyperpolarization-activated cyclic nucleotide-gated (HCN) channels contribute to the rhythmic firing of pacemaker neurons and cardiomyocytes. Mutations in HCN channels are associated with cardiac arrhythmia and epilepsy. HCN channels belong to the superfamily of voltage-gated K+ channels, most of which are activated by depolarization. HCN channels, however, are activated by hyperpolarization. The mechanism behind this reversed gating polarity of HCN channels is not clear. We here show that sea urchin HCN (spHCN) channels with mutations in the C-terminal part of the voltage sensor use the same voltage-sensor movement to either close or open in response to hyperpolarizations depending on the absence or presence of cAMP. Our results support that non-covalent interactions at the C-terminal end of the voltage sensor are critical for HCN gating polarity. These interactions are also critical for the proper closing of the channels because these mutations exhibit large constitutive currents. Since a similar voltage-sensor movement can cause both depolarization- and hyperpolarization-activation in the same channel, this suggests that the coupling between the voltage sensor and the pore is changed to create channels opened by different polarities. We also show an identical voltage-sensor movement in activated and inactivated spHCN channels and suggest a model for spHCN activation and inactivation. Our results suggest the possibility that channels open by opposite voltage dependence, such as HCN and the related EAG channels, use the same voltage-sensor movement but different coupling mechanisms between the voltage sensor and the gate.

Indexed as

Ion Channel GatingPotassium ChannelsCyclic Nucleotide-Gated Cation ChannelsHyperpolarization-Activated Cyclic Nucleotide-Gated ChannelsMutationCyclic Nucleotide-Gated Cation ChannelsHyperpolarization-Activated Cyclic Nucleotide-Gated ChannelsPotassium Channels

Identifiers

PMID36752823
PMCPMC9948645
OpenAlexW4319460981

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.