Evidence map›Paper›PMID 27456671›Full record

ArticleNature communications2016

Protein kinase A modulation of CaV1.4 calcium channels.

Lingjie Sang, Ivy E Dick, David T Yue

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.7field-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

21 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Sudden Death-AssociatedbioRxiv : the preprint server for biology · 2025
    Article
  3. Inactivation of CaV1 and CaV2 channels.The Journal of general physiology · 2025
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Cytosolic peptides encoding CaCommunications biology · 2022
    Article
  10. Advances in the study of axon-associated vesicles.Frontiers in molecular neuroscience · 2022
    Review
  11. Article
  12. Transmission at rod and cone ribbon synapses in the retina.Pflugers Archiv : European journal of physiology · 2021
    Review
  13. Article
  14. Review
  15. Article
  16. Human Osteoblast Migration in DC Electrical Fields Depends on Store Operated CaFrontiers in bioengineering and biotechnology · 2019
    Article
  17. Review
  18. Duplex signaling by CaM and Stac3 enhances CaThe Journal of general physiology · 2018
    Article
  19. Molecular moieties masking CaThe Journal of general physiology · 2018
    Article
  20. Channeling Vision: CaBioMed research international · 2018
    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 1 country.

Lingjie SangCalcium Signals Laboratory, Department of Biomedical Engineering, The Johns Hopkins University School of Medicine, Ross Building, Room 713, 720 Rutland Avenue, Baltimore, Maryland 21205, USA.
Ivy E DickCalcium Signals Laboratory, Department of Biomedical Engineering, The Johns Hopkins University School of Medicine, Ross Building, Room 713, 720 Rutland Avenue, Baltimore, Maryland 21205, USA.
David T YueCalcium Signals Laboratory, Department of Biomedical Engineering, The Johns Hopkins University School of Medicine, Ross Building, Room 713, 720 Rutland Avenue, Baltimore, Maryland 21205, USA.
Johns Hopkins University · USJohns Hopkins Medicine · US

Funding

Translational Research Enhancement CoreP30DK089502 · NIDDK · JOHNS HOPKINS UNIVERSITY · PI ZACHOS, NICHOLAS CONSTANTINE · 2011 to 2020
$12.0M
Chemical biological dissection of Ca2+ entry through Ca2+ channelsR01NS085074 · NINDS · UNIVERSITY OF MARYLAND BALTIMORE · PI DICK, IVY E · 2013 to 2016
$1.3M
NIDDK NIH HHS P30 DK089502NINDS NIH HHS R01 NS085074
6 · The paper itself

Abstract

The regulation of L-type Ca(2+) channels by protein kinase A (PKA) represents a crucial element within cardiac, skeletal muscle and neurological systems. Although much work has been done to understand this regulation in cardiac CaV1.2 Ca(2+) channels, relatively little is known about the closely related CaV1.4 L-type Ca(2+) channels, which feature prominently in the visual system. Here we find that CaV1.4 channels are indeed modulated by PKA phosphorylation within the inhibitor of Ca(2+)-dependent inactivation (ICDI) motif. Phosphorylation of this region promotes the occupancy of calmodulin on the channel, thus increasing channel open probability (PO) and Ca(2+)-dependent inactivation. Although this interaction seems specific to CaV1.4 channels, introduction of ICDI1.4 to CaV1.3 or CaV1.2 channels endows these channels with a form of PKA modulation, previously unobserved in heterologous systems. Thus, this mechanism may not only play an important role in the visual system but may be generalizable across the L-type channel family.

Indexed as

Amino Acid SequenceAnimalsCalcium Channels, L-TypeCyclic AMP-Dependent Protein KinasesEnzyme ActivationGuinea PigsHEK293 CellsHumansPhosphorylationProtein BindingProtein DomainsProtein EngineeringRatsRecombinant ProteinsCACNA1F protein, humanCalcium Channels, L-TypeCyclic AMP-Dependent Protein KinasesRecombinant Proteins

Identifiers

PMID27456671
PMCPMC4963476
OpenAlexW2503210363

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.