Evidence map›Paper›PMID 21708171›Full record

ReviewJournal of molecular and cellular cardiology2012

Calmodulin binding proteins provide domains of local Ca2+ signaling in cardiac myocytes.

Jeffrey J Saucerman, Donald M Bers

Abstract readReview
In one paragraph

Review in Journal of molecular and cellular cardiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

37 citing papers in PubMed, 62 citations in OpenAlex.

  1. Calmodulin mutation N54I causes autosomal dominant CPVT in mice.bioRxiv : the preprint server for biology · 2026
    Article
  2. Review
  3. Review
  4. Review
  5. Article
  6. Feedback contributions to excitation-contraction coupling in native functioning striated muscle.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2023
    Review
  7. Article
  8. Article
  9. Finite element analysis predicts CaScientific reports · 2021
    Article
  10. Dynamic NaeLife · 2021
    Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Store-operated CaCommunications biology · 2018
    Article
  16. Article
  17. Article
  18. Article
  19. Opposing Intermolecular Tuning of CaBiophysical journal · 2017
    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

2 authors at 2 institutions in 1 country.

Jeffrey J SaucermanDepartment of Biomedical Engineering, Robert M. Berne Cardiovascular Research Center, University of Virginia, Charlottesville, VA 22908, USA. jsaucerman@virginia.edu
Donald M Bers
University of California, Davis · USUniversity of Virginia · US

Funding

Program AdministrationP01HL080101 · NHLBI · UNIVERSITY OF CALIFORNIA AT DAVIS · PI BERS, DONALD M · 2006 to 2015
$23.4M
Pathophysiological Regulation of Cardiac Myocyte RyR ChannelR01HL092097 · NHLBI · UNIVERSITY OF CALIFORNIA AT DAVIS · PI Donald M Bers, Robyn T Rebbeck · 2010 to 2026
$9.3M
IONIC CONTROL OF CARDIAC MUSCLE CONTRACTION: EC COUPLINGR37HL030077 · NHLBI · UNIVERSITY OF CALIFORNIA AT DAVIS · PI BERS, DONALD M · 2005 to 2014
$3.9M
IONIC CONTROL OF CARDIAC MUSCLE CONTRACTION: EC COUPLINGR01HL030077 · NHLBI · UNIVERSITY OF CALIFORNIA RIVERSIDE · PI BERS, DONALD M · 1986 to 2018
$3.8M
Quantitative analysis of cAMP compartmentation in heartR01HL094476 · NHLBI · UNIVERSITY OF VIRGINIA · PI SAUCERMAN, JEFFREY J. · 2009 to 2013
$1.8M
NHLBI NIH HHS HL094476NHLBI NIH HHS HL30077NHLBI NIH HHS HL80101NHLBI NIH HHS P01 HL080101NHLBI NIH HHS R01 HL030077NHLBI NIH HHS R01 HL092097NHLBI NIH HHS R01 HL094476NHLBI NIH HHS R37 HL030077
6 · The paper itself

Abstract

Calmodulin (CaM) acts as a common Ca(2+) sensor for many signaling pathways, transducing local Ca(2+) signals into specific cellular outcomes. Many of CaM's signaling functions can be explained by its unique biochemical properties, including high and low affinity Ca(2+)-binding sites with slow and fast kinetics, respectively. CaM is expected to have a limited spatial range of action, emphasizing its role in local Ca(2+) signaling. Interactions with target proteins further fine-tune CaM signal transduction. Here, we focus on only three specific cellular targets for CaM signaling in cardiac myocytes: the L-type Ca(2+) channel, the ryanodine receptor, and the IP(3) receptor. We elaborate a working hypothesis that each channel is regulated by two distinct functional populations of CaM: dedicated CaM and promiscuous CaM. Dedicated CaM is typically tethered to each channel and directly regulates channel activity. In addition, a local pool of promiscuous CaM appears poised to sense local Ca(2+) signals and trigger downstream pathways such as Ca(2+)/CaM dependent-protein kinase II and calcineurin. Understanding how promiscuous CaM coordinates multiple distinct signaling pathways remains a challenge, but is aided by the use of mathematical modeling and a new generation of fluorescent biosensors. This article is part of a special issue entitled "Local Signaling in Myocytes."

Indexed as

AnimalsCalciumCalcium SignalingCalmodulinCalmodulin-Binding ProteinsHumansIon ChannelsMyocytes, CardiacPhosphoric Monoester HydrolasesPhosphotransferasesCalciumCalmodulinCalmodulin-Binding ProteinsIon ChannelsPhosphoric Monoester HydrolasesPhosphotransferases

Identifiers

PMID21708171
PMCPMC3235247
OpenAlexW2045529347

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.