Evidence map›Paper›PMID 35795651›Full record

ReviewFrontiers in physiology2022

Regulation of HCN Channels by Protein Interactions.

Colin H Peters, Rohit K Singh, John R Bankston, Catherine Proenza

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in physiology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

17 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
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  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. The Dysfunction of CaInternational journal of molecular sciences · 2023
    Review
  12. Cannabidiol Modulates M-Type KBiomedicines · 2023
    Article
  13. Novel Functional Features of cGMP Substrate Proteins IRAG1 and IRAG2.International journal of molecular sciences · 2023
    Review
  14. Article
  15. Article
  16. Review
  17. Article
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

4 authors at 1 institution in 1 country.

Colin H PetersDepartment of Physiology and Biophysics, University of Colorado Anschutz Medical Campus, Aurora, CO, United States.
Rohit K SinghDepartment of Physiology and Biophysics, University of Colorado Anschutz Medical Campus, Aurora, CO, United States.
John R BankstonDepartment of Physiology and Biophysics, University of Colorado Anschutz Medical Campus, Aurora, CO, United States.
Catherine ProenzaDepartment of Physiology and Biophysics, University of Colorado Anschutz Medical Campus, Aurora, CO, United States.
University of Colorado Anschutz Medical Campus · US

Funding

Regulation of excitability in sinoatrial myocytesR01HL088427 · NHLBI · UNIVERSITY OF CONNECTICUT STORRS · PI PROENZA, CATHERINE · 2008 to 2024
$5.8M
Dynamics of Acid-sensing ion channelsR35GM137912 · NIGMS · UNIVERSITY OF COLORADO DENVER · PI John Bankston · 2020 to 2026
$2.8M
Allosteric Modulation of HCN ChannelsR01GM140004 · NIGMS · UNIVERSITY OF COLORADO DENVER · PI PROENZA, CATHERINE · 2021 to 2024
$1.7M
NHLBI NIH HHS R01 HL088427NIGMS NIH HHS R01 GM140004NIGMS NIH HHS R35 GM137912
6 · The paper itself

Abstract

Hyperpolarization-activated, cyclic nucleotide-sensitive (HCN) channels are key regulators of subthreshold membrane potentials in excitable cells. The four mammalian HCN channel isoforms, HCN1-HCN4, are expressed throughout the body, where they contribute to diverse physiological processes including cardiac pacemaking, sleep-wakefulness cycles, memory, and somatic sensation. While all HCN channel isoforms produce currents when expressed by themselves, an emerging list of interacting proteins shape HCN channel excitability to influence the physiologically relevant output. The best studied of these regulatory proteins is the auxiliary subunit, TRIP8b, which binds to multiple sites in the C-terminus of the HCN channels to regulate expression and disrupt cAMP binding to fine-tune neuronal HCN channel excitability. Less is known about the mechanisms of action of other HCN channel interaction partners like filamin A, Src tyrosine kinase, and MinK-related peptides, which have a range of effects on HCN channel gating and expression. More recently, the inositol trisphosphate receptor-associated cGMP-kinase substrates IRAG1 and LRMP (also known as IRAG2), were discovered as specific regulators of the HCN4 isoform. This review summarizes the known protein interaction partners of HCN channels and their mechanisms of action and identifies gaps in our knowledge.

Indexed as

accessory proteinsHCN channelsIRAGKCNEprotein subunitsTRIP8b

Identifiers

PMID35795651
PMCPMC9251338
OpenAlexW4283163958

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.