Evidence map›Paper›PMID 27742556›Full record

ReviewJournal of molecular and cellular cardiology2016

Role of myosin light chain phosphatase in cardiac physiology and pathophysiology.

Audrey N Chang, Kristine E Kamm, James T Stull

Open access · greenAbstract readReview
In one paragraph

Review in Journal of molecular and cellular cardiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.6field-weighted citation impact, top 15% 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

27 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Spatial control of myosin regulatory light chain phosphorylation modulates cardiac thick filament mechanosensing.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  6. Loss ofCurrent issues in molecular biology · 2025
    Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Cardiac muscle physiology.BJA education · 2023
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Regulation of myosin light-chain phosphorylation and its roles in cardiovascular physiology and pathophysiology.Hypertension research : official journal of the Japanese Society of Hypertension · 2022
    Review
  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

3 authors at 1 institution in 1 country.

Audrey N ChangDepartment of Physiology, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA. Electronic address: audreyn.chang@utsouthwestern.edu.
Kristine E KammDepartment of Physiology, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.
James T StullDepartment of Physiology, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.
The University of Texas Southwestern Medical Center · US

Funding

Pathology and Molecular Imaging CoreP01HL110869 · NHLBI · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI MILEWICZ, DIANNA M · 2012 to 2016
$10.4M
Signal transduction mechanisms to myosin phosphataseR01HL112778 · NHLBI · UT SOUTHWESTERN MEDICAL CENTER · PI STULL, JAMES T · 2013 to 2016
$1.6M
NHLBI NIH HHS P01 HL110869NHLBI NIH HHS R01 HL112778
6 · The paper itself

Abstract

Maintenance of contractile performance of the heart is achieved in part by the constitutive 40% phosphorylation of myosin regulatory light chain (RLC) in sarcomeres. The importance of this extent of RLC phosphorylation for optimal cardiac performance becomes apparent when various mouse models and resultant phenotypes are compared. The absence or attenuation of RLC phosphorylation results in poor performance leading to heart failure, whereas increased RLC phosphorylation is associated with cardiac protection from stresses. Although information is limited, RLC phosphorylation appears compromised in human heart failure which is consistent with data from mouse studies. The extent of cardiac RLC phosphorylation is determined by the balanced activities of cardiac myosin light chain kinases and phosphatases, the regulatory mechanisms of which are now emerging. This review thusly focuses on kinases that may participate in phosphorylating RLC to make the substrate for cardiac myosin light chain phosphatases, in addition to providing perspectives on the family of myosin light chain phosphatases and involved signaling mechanisms. Because biochemical and physiological information about cardiac myosin light chain phosphatase is sparse, such studies represent an emerging area of investigation in health and disease.

Indexed as

AnimalsHeartHeart DiseasesHumansMyocardial ContractionMyocardiumMyosin-Light-Chain KinaseMyosin-Light-Chain PhosphataseMyosin Light ChainsPhosphoric Monoester HydrolasesPhosphorylationProtein BindingProtein Interaction Domains and MotifsSarcomeresSignal TransductionStructure-Activity RelationshipMyosin-Light-Chain KinaseMyosin-Light-Chain PhosphataseMyosin Light ChainsPhosphoric Monoester HydrolasesCardiac contractionMyosinMyosin light chain kinaseMyosin light chain phosphataseRegulatory light chainSarcomere

Identifiers

PMID27742556
PMCPMC5154923
OpenAlexW2531224311

What OpenQuestion holds

Textmetadata
LicenceTDM
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.