Evidence map›Paper›PMID 35238659›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2022

Structures of the junctophilin/voltage-gated calcium channel interface reveal hot spot for cardiomyopathy mutations.

Zheng Fang Yang, Pankaj Panwar, Ciaran R McFarlane, Wietske E Tuinte, Marta Campiglio, Filip Van Petegem

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.9field-weighted citation impact, top 8% 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

24 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Nanoscale architecture and dynamics of CaJournal of molecular and cellular cardiology plus · 2025
    Article
  7. Article
  8. Article
  9. Nonstructural Roles of Junctophilin-2 in the Heart.JACC. Basic to translational science · 2025
    Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. CaCommunications biology · 2024
    Article
  15. Voltage-induced calcium release inProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  16. Review
  17. Article
  18. Review
  19. Article
  20. CaHandbook of experimental pharmacology · 2023
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 2 countries.

Zheng Fang YangDepartment of Biochemistry and Molecular Biology, The Life Sciences Institute, University of British Columbia, Vancouver, BC V6T 1Z3, Canada.ORCID 0000-0002-7681-3142
Pankaj PanwarDepartment of Biochemistry and Molecular Biology, The Life Sciences Institute, University of British Columbia, Vancouver, BC V6T 1Z3, Canada.
Ciaran R McFarlaneDepartment of Biochemistry and Molecular Biology, The Life Sciences Institute, University of British Columbia, Vancouver, BC V6T 1Z3, Canada.
Wietske E TuinteInstitute of Physiology, Medical University of Innsbruck, Innsbruck, 6020 Austria.ORCID 0000-0003-0331-0402
Marta CampiglioInstitute of Physiology, Medical University of Innsbruck, Innsbruck, 6020 Austria.ORCID 0000-0002-9629-2073
Filip Van PetegemDepartment of Biochemistry and Molecular Biology, The Life Sciences Institute, University of British Columbia, Vancouver, BC V6T 1Z3, Canada.ORCID 0000-0003-2728-8537
University of British Columbia · CAInnsbruck Medical University · AT

Funding

Austrian Science Fund FWF DOC 30
6 · The paper itself

Abstract

SignificanceIon channels have evolved the ability to communicate with one another, either through protein-protein interactions, or indirectly via intermediate diffusible messenger molecules. In special cases, the channels are part of different membranes. In muscle tissue, the T-tubule membrane is in proximity to the sarcoplasmic reticulum, allowing communication between L-type calcium channels and ryanodine receptors. This process is critical for excitation-contraction coupling and requires auxiliary proteins like junctophilin (JPH). JPHs are targets for disease-associated mutations, most notably hypertrophic cardiomyopathy mutations in the JPH2 isoform. Here we provide high-resolution snapshots of JPH, both alone and in complex with a calcium channel peptide, and show how this interaction is targeted by cardiomyopathy mutations.

Indexed as

Ion Channel GatingMutationCalcium Channels, L-TypeCardiomyopathy, HypertrophicCrystallography, X-RayHumansProtein ConformationProtein IsoformsCalcium Channels, L-TypeProtein Isoformscalcium releasecalcium signalingcardiomyopathyion channelsmuscle excitation–contraction coupling

Identifiers

PMID35238659
PMCPMC8916002
OpenAlexW4214913497

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.