Evidence map›Paper›PMID 19473981›Full record

ArticleThe Journal of biological chemistry2009

Determinants in CaV1 channels that regulate the Ca2+ sensitivity of bound calmodulin.

D Brent Halling, Dimitra K Georgiou, D J Black, Guojun Yang, Jennifer L Fallon, Florante A Quiocho, Steen E Pedersen, Susan L Hamilton

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
–field-weighted citation impact
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

30 citing papers in PubMed.

  1. Article
  2. Article
  3. Calcium channels as pharmacological targets for cancer therapy.Clinical and experimental medicine · 2025
    Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Crystal structures of CaProceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  14. Duplex signaling by CaM and Stac3 enhances CaThe Journal of general physiology · 2018
    Article
  15. Article
  16. Article
  17. Opposing Intermolecular Tuning of CaBiophysical journal · 2017
    Article
  18. Article
  19. Review
  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

8 authors.

D Brent HallingDepartment of Molecular Physiology and Biophysics, Baylor College of Medicine, Houston, Texas 77030, USA.
Dimitra K Georgiou
D J Black
Guojun Yang
Jennifer L Fallon
Florante A Quiocho
Steen E Pedersen
Susan L Hamilton

Funding

MOLECULAR DETERMINANTS OF E-C COUPLINGR01AR044864 · NIAMS · BAYLOR COLLEGE OF MEDICINE · PI HAMILTON, SUSAN L · 1999 to 2008
$4.0M
Regulation of Calcium Channels by CalmodulinR01HL087099 · NHLBI · BAYLOR COLLEGE OF MEDICINE · PI PEDERSEN, STEEN E · 2008 to 2011
$1.5M
SOLUTE TRANSPORT TAXIS AND SENSORY PATHWAY RECEPTORSR01GM021371 · NIGMS · RICE UNIVERSITY · PI QUIOCHO, FLORANTE A · 1985 to 2006
$1.4M
NHLBI NIH HHS HL087099NHLBI NIH HHS R01 HL087099NIAMS NIH HHS AR44864NIAMS NIH HHS R01 AR044864NIGMS NIH HHS GM021371NIGMS NIH HHS R01 GM021371
6 · The paper itself

Abstract

Calmodulin binds to IQ motifs in the alpha(1) subunit of Ca(V)1.1 and Ca(V)1.2, but the affinities of calmodulin for the motif and for Ca(2+) are higher when bound to Ca(V)1.2 IQ. The Ca(V)1.1 IQ and Ca(V)1.2 IQ sequences differ by four amino acids. We determined the structure of calmodulin bound to Ca(V)1.1 IQ and compared it with that of calmodulin bound to Ca(V)1.2 IQ. Four methionines in Ca(2+)-calmodulin form a hydrophobic binding pocket for the peptide, but only one of the four nonconserved amino acids (His-1532 of Ca(V)1.1 and Tyr-1675 of Ca(V)1.2) contacts this calmodulin pocket. However, Tyr-1675 in Ca(V)1.2 contributes only modestly to the higher affinity of this peptide for calmodulin; the other three amino acids in Ca(V)1.2 contribute significantly to the difference in the Ca(2+) affinity of the bound calmodulin despite having no direct contact with calmodulin. Those residues appear to allow an interaction with calmodulin with one lobe Ca(2+)-bound and one lobe Ca(2+)-free. Our data also provide evidence for lobe-lobe interactions in calmodulin bound to Ca(V)1.2.

Indexed as

Amino Acid MotifsAmino Acid SequenceAnimalsCalciumCalcium Channels, L-TypeCalmodulinCrystallography, X-RayHumansMammalsModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedPeptidesProtein BindingProtein ConformationCalciumCalcium Channels, L-TypeCalmodulinPeptides

Identifiers

PMID19473981
PMCPMC2740430

What OpenQuestion holds

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Registered trials

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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.