Evidence map›Paper›PMID 32140110›Full record

ReviewFrontiers in physiology2020

Palmitoylation: A Fatty Regulator of Myocardial Electrophysiology.

Kobina Essandoh, Julie M Philippe, Paul M Jenkins, Matthew J Brody

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in physiology, 2020. 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
2.3field-weighted citation impact, top 11% 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, 40 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Palmitoylation in cardiovascular diseases: Molecular mechanism and therapeutic potential.International journal of cardiology. Heart & vasculature · 2025
    Review
  8. Article
  9. Review
  10. Article
  11. Review
  12. Metabolite signaling in the heart.Nature cardiovascular research · 2023
    Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Proteome-wide identification of palmitoylated proteins in mouse testis.Reproductive sciences (Thousand Oaks, Calif.) · 2022
    Article
  19. Article
  20. 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.

Kobina EssandohDepartment of Pharmacology, University of Michigan, Ann Arbor, MI, United States.
Julie M PhilippeDepartment of Pharmacology, University of Michigan, Ann Arbor, MI, United States.
Paul M JenkinsDepartment of Pharmacology, University of Michigan, Ann Arbor, MI, United States.
Matthew J BrodyDepartment of Pharmacology, University of Michigan, Ann Arbor, MI, United States.
University of Michigan–Ann Arbor · US

Funding

The role of palmitoylation in cardiac signal transduction and disease pathogenesisR00HL136695 · NHLBI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI BRODY, MATTHEW JACOB · 2019 to 2021
$747k
NHLBI NIH HHS R00 HL136695
6 · The paper itself

Abstract

Regulation of cardiac physiology is well known to occur through the action of kinases that reversibly phosphorylate ion channels, calcium handling machinery, and signaling effectors. However, it is becoming increasingly apparent that palmitoylation or S-acylation, the post-translational modification of cysteines with saturated fatty acids, plays instrumental roles in regulating the localization, activity, stability, sorting, and function of numerous proteins, including proteins known to have essential functions in cardiomyocytes. However, the impact of this modification on cardiac physiology requires further investigation. S-acylation is catalyzed by the zDHHC family of S-acyl transferases that localize to intracellular organelle membranes or the sarcolemma. Recent work has begun to uncover functions of S-acylation in the heart, particularly in the regulation of cardiac electrophysiology, including modification of the sodium-calcium exchanger, phospholemman and the cardiac sodium pump, as well as the voltage-gated sodium channel. Elucidating the regulatory functions of zDHHC enzymes in cardiomyocytes and determination of how S-acylation is altered in the diseased heart will shed light on how these modifications participate in cardiac pathogenesis and potentially identify novel targets for the treatment of cardiovascular disease. Indeed, proteins with critical signaling roles in the heart are also S-acylated, including receptors and G-proteins, yet the dynamics and functions of these modifications in myocardial physiology have not been interrogated. Here, we will review what is known about zDHHC enzymes and substrate S-acylation in myocardial physiology and highlight future areas of investigation that will uncover novel functions of S-acylation in cardiac homeostasis and pathophysiology.

Indexed as

cardiac physiologyelectrophysiologyion channelsmyocardiumpalmitoylationpost-translational modificationsS-acylationzDHHC enzymes

Identifiers

PMID32140110
PMCPMC7042378
OpenAlexW3007286922

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.