Evidence map›Paper›PMID 19351515›Full record

ReviewProgress in biophysics and molecular biology

Regulation of cardiac excitation and contraction by p21 activated kinase-1.

Yunbo Ke, Ming Lei, R John Solaro

Open access · greenAbstract readReview
In one paragraph

Review in Progress in biophysics and molecular biology. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

29 citing papers in PubMed, 54 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Review
  6. Cardiomyocyte electrophysiology and its modulation: current views and future prospects.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2023
    Review
  7. Review
  8. Review
  9. Article
  10. Cyclic AMP-dependent protein kinase A and EPAC mediate VIP and secretin stimulation of PAK4 and activation of NaAmerican journal of physiology. Gastrointestinal and liver physiology · 2019
    Article
  11. Review
  12. Regulation of cardiac gap junctions by protein phosphatases.Journal of molecular and cellular cardiology · 2017
    Review
  13. Review
  14. Review
  15. Review
  16. Article
  17. Review
  18. Mechanosensing and Regulation of Cardiac Function.Journal of clinical & experimental cardiology · 2014
    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

3 authors at 2 institutions in 2 countries.

Yunbo KeThe Department of Physiology and Biophysics and Center for Cardiovascular Research, University of Illinois at Chicago, College of Medicine, Room 202, COMRB, 835 South Wolcott Avenue, Chicago, IL 60612, USA.
Ming Lei
R John Solaro
University of Illinois Chicago · USUniversity of Manchester · GB

Funding

Sarcomeric Modifications and Progressive Cardiac MaladaptationP01HL062426 · NHLBI · UNIVERSITY OF ILLINOIS AT CHICAGO · PI DE TOMBE, PIETER P. · 2000 to 2020
$42.4M
Troponin Mudulation in Heart FailureR01HL064035 · NHLBI · UNIVERSITY OF ILLINOIS AT CHICAGO · PI SOLARO, R JOHN, WOLSKA, BEATA M. · 2000 to 2013
$4.7M
MODULATION OF CALCIUM CONTROL OF CARDIAC MYOFIBRILSR01HL022231 · NHLBI · UNIVERSITY OF ILLINOIS AT CHICAGO · PI GUPTA, MADHU, SOLARO, R JOHN · 1985 to 2014
$2.9M
NHLBI NIH HHS P01 HL062426NHLBI NIH HHS R01 HL022231NHLBI NIH HHS R01 HL064035
6 · The paper itself

Abstract

Cardiac excitation and contraction are regulated by a variety of signaling molecules. Central to the regulatory scheme are protein kinases and phosphatases that carry out reversible phosphorylation of different effectors. The process of beta-adrenergic stimulation mediated by cAMP dependent protein kinase (PKA) forms a well-known pathway considered as the most significant control mechanism in excitation and contraction as well as many other regulatory mechanisms in cardiac function. However, although dephosphorylation pathways are critical to these regulatory processes, signaling to phosphatases is relatively poorly understood. Emerging evidence indicates that regulation of phosphatases, which dampen the effect of beta-adrenergic stimulation, is also important. We review here functional studies of p21 activated kinase-1 (Pak1) and its potential role as an upstream signal for protein phosphatase PP2A in the heart. Pak1 is a serine/threonine protein kinase directly activated by the small GTPases Cdc42 and Rac1. Pak1 is highly expressed in different regions of the heart and modulates the activities of ion channels, sarcomeric proteins, and other phosphoproteins through up-regulation of PP2A activity. Coordination of Pak1 and PP2A activities is not only potentially involved in regulation of normal cardiac function, but is likely to be important in patho-physiological conditions.

Indexed as

AnimalsArrhythmias, CardiacDimerizationElectrophysiological PhenomenaHumansMiceModels, CardiovascularMyocardial ContractionMyocardial IschemiaMyocardiump21-Activated KinasesPhosphorylationProtein Phosphatase 2Signal Transductionp21-Activated KinasesPAK1 protein, humanPak1 protein, mouseProtein Phosphatase 2

Identifiers

PMID19351515
PMCPMC2709768
OpenAlexW2080442209

What OpenQuestion holds

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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.