Evidence map›Paper›PMID 16939418›Full record

ArticleThe Biochemical journal2007

Binding of calcium ions and SNAP-25 to the hexa EF-hand protein secretagogin.

Annika Rogstam, Sara Linse, Anders Lindqvist, Peter James, Ludwig Wagner, Tord Berggård

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
1.1field-weighted citation impact, top 25% 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

56 citing papers in PubMed, 91 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Neuronal activity modulates the expression of secretagogin, a CaActa physiologica (Oxford, England) · 2025
    Article
  5. A hydrophobic groove in secretagogin allows for alternate interactions with SNAP-25 and syntaxin-4 in endocrine tissues.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  6. Article
  7. SCGN deficiency is a risk factor for autism spectrum disorder.Signal transduction and targeted therapy · 2023
    Article
  8. Article
  9. Article
  10. Article
  11. Structural and mechanistic insights into secretagogin-mediated exocytosis.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  12. Article
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  15. Brain-wide genetic mapping identifies the indusium griseum as a prenatal target of pharmacologically unrelated psychostimulants.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  16. Article
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  18. eLife · 2019
    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

6 authors at 2 institutions in 2 countries.

Annika RogstamDepartment of Biophysical Chemistry, Lund University, P.O. Box 124, SE-221 00 Lund, Sweden.
Sara Linse
Anders Lindqvist
Peter James
Ludwig Wagner
Tord Berggård
Lund University · SEUniversity of Vienna · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Secretagogin is a hexa EF-hand protein, which has been identified as a novel potential tumour marker. In the present study, we show that secretagogin binds four Ca2+ ions (log K1=7.1+/-0.4, log K2=4.7+/-0.6, log K3=3.6+/-0.7 and log K4=4.6+/-0.6 in physiological salt buffers) with a [Ca2+](0.5) of approx. 25 microM. The tertiary structure of secretagogin changes significantly upon Ca2+ binding, but not upon Mg2+ binding, and the amount of exposed hydrophobic surface in secretagogin increases upon Ca2+ binding, but not upon Mg2+ binding. These properties suggest that secretagogin belongs to the 'sensor' family of Ca2+-binding proteins. However, in contrast with the prototypical Ca2+ sensor calmodulin, which interacts with a very large number of proteins, secretagogin is significantly less promiscuous. Only one secretagogin-interacting protein was reproducibly identified from insulinoma cell lysates and from bovine and mouse brain homogenates. This protein was identified as SNAP-25 (25 kDa synaptosome-associated protein), a protein involved in Ca2+-induced exocytosis in neurons and in neuroendocrine cells. K(d) was determined to be 1.2x10(-7) M in the presence of Ca2+ and 1.5x10(-6) M in the absence of Ca2+. The comparatively low Ca2+ affinity for secretagogin and the fact that it undergoes Ca2+-induced conformational changes and interacts with SNAP-25 raise the possibility that secretagogin may link Ca2+ signalling to exocytotic processes.

Indexed as

CalciumCalcium-Binding ProteinsCalorimetryCircular DichroismHumansKineticsModels, MolecularProtein BindingProtein ConformationSecretagoginsSignal TransductionSpectrophotometry, UltravioletSynaptosomal-Associated Protein 25SynaptosomesTryptophanCalciumCalcium-Binding ProteinsSCGN protein, humanSecretagoginsSNAP25 protein, humanSynaptosomal-Associated Protein 25Tryptophan

Identifiers

PMID16939418
PMCPMC1698678
OpenAlexW2048057151

What OpenQuestion holds

Textmetadata
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.