Evidence map›Paper›PMID 10958666›Full record

ArticleMolecular and cellular biology2000

A homolog of voltage-gated Ca(2+) channels stimulated by depletion of secretory Ca(2+) in yeast.

E G Locke, M Bonilla, L Liang, Y Takita, K W Cunningham

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 92 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
92citing papers in PubMed, 1 pooled it
4.2field-weighted citation impact, top 5% 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

92 citing papers in PubMed, 1 synthesis or guideline pooled it, 216 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Article
  6. High-Affinity Plasma Membrane CaInternational journal of molecular sciences · 2024
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  8. Modeling Calcium Signaling inFrontiers in molecular biosciences · 2022
    Article
  9. Review
  10. Review
  11. Cation Transporters ofBiomolecules · 2021
    Review
  12. Origins of eukaryotic excitability.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2021
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Possible Role of the CaMolecules (Basel, Switzerland) · 2019
    Article
  18. Article
  19. Review
  20. Article

32 more citing papers are in PubMed but not listed here.

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

5 authors at 1 institution in 1 country.

E G LockeDepartment of Biology, Johns Hopkins University, Baltimore, Maryland 21218, USA.
M Bonilla
L Liang
Y Takita
K W Cunningham
Johns Hopkins University · US

Funding

CALCIUM SIGNALING AND TRANSPORT IN S CEREVISIAER01GM053082 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI CUNNINGHAM, KYLE W · 1996 to 2008
$2.8M
NIGMS NIH HHS GM53083NIGMS NIH HHS R01 GM053082
6 · The paper itself

Abstract

In animal cells, capacitative calcium entry (CCE) mechanisms become activated specifically in response to depletion of calcium ions (Ca(2+)) from secretory organelles. CCE serves to replenish those organelles and to enhance signaling pathways that respond to elevated free Ca(2+) concentrations in the cytoplasm. The mechanism of CCE regulation is not understood because few of its essential components have been identified. We show here for the first time that the budding yeast Saccharomyces cerevisiae employs a CCE-like mechanism to refill Ca(2+) stores within the secretory pathway. Mutants lacking Pmr1p, a conserved Ca(2+) pump in the secretory pathway, exhibit higher rates of Ca(2+) influx relative to wild-type cells due to the stimulation of a high-affinity Ca(2+) uptake system. Stimulation of this Ca(2+) uptake system was blocked in pmr1 mutants by expression of mammalian SERCA pumps. The high-affinity Ca(2+) uptake system was also stimulated in wild-type cells overexpressing vacuolar Ca(2+) transporters that competed with Pmr1p for substrate. A screen for yeast mutants specifically defective in the high-affinity Ca(2+) uptake system revealed two genes, CCH1 and MID1, previously implicated in Ca(2+) influx in response to mating pheromones. Cch1p and Mid1p were localized to the plasma membrane, coimmunoprecipitated from solubilized membranes, and shown to function together within a single pathway that ensures that adequate levels of Ca(2+) are supplied to Pmr1p to sustain secretion and growth. Expression of Cch1p and Mid1p was not affected in pmr1 mutants. The evidence supports the hypothesis that yeast maintains a homeostatic mechanism related to CCE in mammalian cells. The homology between Cch1p and the catalytic subunit of voltage-gated Ca(2+) channels raises the possibility that in some circumstances CCE in animal cells may involve homologs of Cch1p and a conserved regulatory mechanism.

Indexed as

Calcium-Transporting ATPasesSaccharomyces cerevisiae ProteinsATP-Binding Cassette TransportersCalciumCalcium ChannelsFungal ProteinsIon Channel GatingMembrane GlycoproteinsMolecular ChaperonesMutagenesisSaccharomyces cerevisiaeVacuolesATP-Binding Cassette TransportersCalciumCalcium ChannelsCalcium-Transporting ATPasesCCH1 protein, S cerevisiaeFungal ProteinsMembrane GlycoproteinsMID1 protein, S cerevisiaeMolecular ChaperonesSaccharomyces cerevisiae ProteinsSSC1 protein, S cerevisiae

Identifiers

PMID10958666
PMCPMC86178
OpenAlexW2157275644

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.