Evidence map›Paper›PMID 16734434›Full record

ArticleBiochemistry2006

Biphasic Ca2+-dependent switching in a calmodulin-IQ domain complex.

D J Black, Jared Leonard, Anthony Persechini

Abstract read
In one paragraph

Article in Biochemistry, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing 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

24 citing papers in PubMed.

  1. NaStructure (London, England : 1993) · 2021
    Article
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  8. Calcineurin determines toxic versus beneficial responses to α-synuclein.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  9. Visualizing CaMKII and CaM activity: a paradigm of compartmentalized signaling.Journal of molecular medicine (Berlin, Germany) · 2013
    Review
  10. NMR studies of the interaction of calmodulin with IQ motif peptides.Methods in molecular biology (Clifton, N.J.) · 2013
    Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
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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.

D J BlackDivision of Molecular Biology and Biochemistry, University of Missouri, Kansas City, Missouri 64110-2499, USA.
Jared Leonard
Anthony Persechini

Funding

Switching Kinetics in Calmodulin-IQ Domain ComplexesR01GM074887 · NIGMS · UNIVERSITY OF MISSOURI KANSAS CITY · PI PERSECHINI, ANTHONY J · 2006 to 2009
$899k
NIGMS NIH HHS GM074887NIGMS NIH HHS R01 GM074887
6 · The paper itself

Abstract

The relationship between the free Ca2+ concentration and the apparent dissociation constant for the complex between calmodulin (CaM) and the neuromodulin IQ domain consists of two phases. In the first phase, Ca2+ bound to the C-ter EF hand pair in CaM increases the Kd for the complex from the Ca2+-free value of 2.3 +/- 0.1 microM to a value of 14.4 +/- 1.3 microM. In the second phase, Ca2+ bound to the N-ter EF hand pair reduces the Kd for the complex to a value of 2.5 +/- 0.1 microM, reversing the effect of the first phase. Due to energy coupling effects associated with these phases, the mean dissociation constant for binding of Ca2+ to the C-ter EF hand pair is increased approximately 3-fold, from 1.8 +/- 0.1 to 5.1 +/- 0.7 microM, and the mean dissociation constant for binding of Ca2+ to the N-ter EF hand pair is decreased by the same factor, from 11.2 +/- 1.0 to 3.5 +/- 0.6 microM. These characteristics produce a bell-shaped relationship between the apparent dissociation constant for the complex and the free Ca2+ concentration, with a distance of 5-6 microM between the midpoints of the rising and falling phases. Release of CaM from the neuromodulin IQ domain therefore appears to be promoted over a relatively narrow range of free Ca2+ concentrations. Our results demonstrate that CaM-IQ domain complexes can function as biphasic Ca2+ switches through opposing effects of Ca2+ bound sequentially to the two EF hand pairs in CaM.

Indexed as

CalciumCalmodulinCalmodulin-Binding ProteinsGAP-43 ProteinMutationProtein ConformationProtein Structure, TertiaryBSCaMIQ peptideCalciumCalmodulinCalmodulin-Binding ProteinsGAP-43 Protein

Identifiers

PMID16734434
PMCPMC2532102

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.