Evidence map›Paper›PMID 35001666›Full record

ReviewPhysiological reviews2022

The role of junctophilin proteins in cellular function.

Stephan E Lehnart, Xander H T Wehrens

Open access · greenAbstract readReview
In one paragraph

Review in Physiological reviews, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
4.9field-weighted citation impact, top 3% 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

44 citing papers in PubMed, 58 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Sex-specific phosphoproteome responses to calorie restriction and insulin in skeletal muscle from older rats.The journals of gerontology. Series A, Biological sciences and medical sciences · 2025
    Article
  10. Nonstructural Roles of Junctophilin-2 in the Heart.JACC. Basic to translational science · 2025
    Review
  11. Review
  12. Observational
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Nanoscale organization of cardiac calcium channels is dependent on thyroid hormone status.American journal of physiology. Heart and circulatory physiology · 2024
    Article
  19. Article
  20. Review
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

2 authors at 2 institutions in 2 countries.

Stephan E LehnartCellular Biophysics and Translational Cardiology Section, Heart Research Center Göttingen, University Medical Center Göttingen, Georg-August University Göttingen, Göttingen, Germany.ORCID 0000-0002-8115-3513
Xander H T WehrensCardiovascular Research Institute, Baylor College of Medicine, Houston, Texas.ORCID 0000-0001-5044-672X
Baylor College of Medicine · USUniversitätsmedizin Göttingen · DE

Funding

Regulation of Sarcoplasmic Reticulum Calcium Release in Heart FailureR01HL091947 · NHLBI · BAYLOR COLLEGE OF MEDICINE · PI WEHRENS, XANDER H.T. · 2009 to 2019
$3.2M
Defining novel mechanisms for regulation of atrial INa and arrhythmiasR01HL134824 · NHLBI · OHIO STATE UNIVERSITY · PI HUND, THOMAS JEFFREY, MOHLER, PETER J. · 2017 to 2020
$3.0M
Determining the Role of Junctophilin-2 in Cardiac DiseaseR01HL117641 · NHLBI · BAYLOR COLLEGE OF MEDICINE · PI WEHRENS, XANDER H.T. · 2014 to 2017
$2.3M
Mechanisms underlying atrial fibrillation associated with chronic kidney diseaseR01HL147108 · NHLBI · BAYLOR COLLEGE OF MEDICINE · PI LI, NA, WEHRENS, XANDER H.T. · 2019 to 2022
$2.0M
NHLBI NIH HHS R01 HL091947NHLBI NIH HHS R01 HL117641NHLBI NIH HHS R01 HL134824NHLBI NIH HHS R01 HL147108
6 · The paper itself

Abstract

Junctophilins (JPHs) comprise a family of structural proteins that connect the plasma membrane to intracellular organelles such as the endo/sarcoplasmic reticulum (ER/SR). Tethering of these membrane structures results in the formation of highly organized subcellular junctions that play important signaling roles in all excitable cell types. There are four JPH isoforms, expressed primarily in muscle and neuronal cell types. Each JPH protein consists of six membrane occupation and recognition nexus (MORN) motifs, a joining region connecting these to another set of two MORN motifs, a putative alpha-helical region, a divergent region exhibiting low homology between JPH isoforms, and a carboxy-terminal transmembrane region anchoring into the ER/SR membrane. JPH isoforms play essential roles in developing and maintaining subcellular membrane junctions. Conversely, inherited mutations in JPH2 cause hypertrophic or dilated cardiomyopathy, while trinucleotide expansions in the JPH3 gene cause Huntington Disease-Like 2. Loss of JPH1 protein levels can cause skeletal myopathy, while loss of cardiac JPH2 levels causes heart failure and atrial fibrillation, among other disease. This review will provide a comprehensive overview of the JPH gene family, phylogeny, and evolutionary analysis of JPH genes and other MORN domain proteins. JPH biogenesis, membrane tethering, and binding partners will be discussed, as well as functional roles of JPH isoforms in excitable cells. Finally, potential roles of JPH isoform deficits in human disease pathogenesis will be reviewed.

Indexed as

Membrane ProteinsMuscular DiseasesCell MembraneCell Physiological PhenomenaHumansjunctophilinMembrane Proteinscardiomyopathyexcitation-contraction couplingheart failurejunctophilins

Identifiers

PMID35001666
PMCPMC8934682
OpenAlexW4205896120

What Socratic 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 Socratic graph.