Evidence map›Paper›PMID 14676285›Full record

ArticleThe Journal of general physiology2004

Changes in local S4 environment provide a voltage-sensing mechanism for mammalian hyperpolarization-activated HCN channels.

Damian C Bell, Huan Yao, Renee C Saenger, John H Riley, Steven A Siegelbaum

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of general physiology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

49 citing papers in PubMed, 85 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review: HCN Channels in the Heart.Current cardiology reviews · 2022
    Review
  5. A second S4 movement opens hyperpolarization-activated HCN channels.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Bipolar switching by HCN voltage sensor underlies hyperpolarization activation.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  11. Insights into the molecular mechanism for hyperpolarization-dependent activation of HCN channels.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Damian C BellCenter for Neurobiology & Behavior, Howard Hughes Medical Institute, Columbia University, New York, NY 10032, USA.
Huan Yao
Renee C Saenger
John H Riley
Steven A Siegelbaum
Howard Hughes Medical Institute · US

Funding

Regulation of HCN channel trafficking and function in the brain by TRIP8bR01NS036658 · NINDS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI SIEGELBAUM, STEVEN A · 1998 to 2016
$4.5M
Regulation of HCN channel trafficking and function in the brain by TRIP8bR56NS036658 · NINDS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI SIEGELBAUM, STEVEN A · 2012 to 2012
$398k
NINDS NIH HHS NS36658NINDS NIH HHS R01 NS036658NINDS NIH HHS R56 NS036658Wellcome Trust
6 · The paper itself

Abstract

The positively charged S4 transmembrane segment of voltage-gated channels is thought to function as the voltage sensor by moving charge through the membrane electric field in response to depolarization. Here we studied S4 movements in the mammalian HCN pacemaker channels. Unlike most voltage-gated channel family members that are activated by depolarization, HCN channels are activated by hyperpolarization. We determined the reactivity of the charged sulfhydryl-modifying reagent, MTSET, with substituted cysteine (Cys) residues along the HCN1 S4 segment. Using an HCN1 channel engineered to be MTS resistant except for the chosen S4 Cys substitution, we determined the reactivity of 12 S4 residues to external or internal MTSET application in either the closed or open state of the channel. Cys substitutions in the NH2-terminal half of S4 only reacted with external MTSET; the rates of reactivity were rapid, regardless of whether the channel was open or closed. In contrast, Cys substitutions in the COOH-terminal half of S4 selectively reacted with internal MTSET when the channel was open. In the open state, the boundary between externally and internally accessible residues was remarkably narrow (approximately 3 residues). This suggests that S4 lies in a water-filled gating canal with a very narrow barrier between the external and internal solutions, similar to depolarization-gated channels. However, the pattern of reactivity is incompatible with either classical gating models, which postulate a large translational or rotational movement of S4 within a gating canal, or with a recent model in which S4 forms a peripheral voltage-sensing paddle (with S3b) that moves within the lipid bilayer (the KvAP model). Rather, we suggest that voltage sensing is due to a rearrangement in transmembrane segments surrounding S4, leading to a collapse of an internal gating canal upon channel closure that alters the shape of the membrane field around a relatively static S4 segment.

Indexed as

AnimalsCell MembraneCyclic Nucleotide-Gated Cation ChannelsCysteineElectrophysiologyHyperpolarization-Activated Cyclic Nucleotide-Gated ChannelsIon Channel GatingIon ChannelsMammalsMembrane PotentialsMesylatesOocytesPotassium ChannelsPotassium Channels, Voltage-GatedSulfhydryl ReagentsXenopus(2-(trimethylammonium)ethyl)methanethiosulfonateCyclic Nucleotide-Gated Cation ChannelsCysteineHyperpolarization-Activated Cyclic Nucleotide-Gated ChannelsIon ChannelsMesylatesPotassium ChannelsPotassium Channels, Voltage-GatedSulfhydryl Reagents

Identifiers

PMID14676285
PMCPMC2217414
OpenAlexW2091356227

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.