Evidence map›Paper›PMID 21764990›Full record

ArticleThe Plant cell2011

A novel calcium binding site in the slow vacuolar cation channel TPC1 senses luminal calcium levels.

Beata Dadacz-Narloch, Diana Beyhl, Christina Larisch, Enrique J López-Sanjurjo, Ralf Reski, Kazuyuki Kuchitsu, Thomas D Müller, Dirk Becker, Gerald Schönknecht, Rainer Hedrich

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
7.9field-weighted citation impact, top 2% 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

50 citing papers in PubMed, 97 citations in OpenAlex.

  1. Review
  2. Article
  3. Arabidopsis HAK5 under low KNature communications · 2024
    Article
  4. eLife · 2023
    Article
  5. Article
  6. Structure and Function of Plant and Mammalian TPC Channels.Handbook of experimental pharmacology · 2023
    Article
  7. TPC1-Type Channels inPlants (Basel, Switzerland) · 2022
    Article
  8. Review
  9. Molecular basis of multistep voltage activation in plant two-pore channel 1.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  10. Review
  11. Review
  12. Article
  13. Voltage-gating and cytosolic CaProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  14. Review
  15. Article
  16. Review
  17. Article
  18. Evolutionary Aspects of TRPMLs and TPCs.International journal of molecular sciences · 2020
    Review
  19. Salt Stress Signals on Demand: Cellular Events in the Right Context.International journal of molecular sciences · 2020
    Review
  20. Resting state structure of the hyperdepolarization activated two-pore channel 3.Proceedings of the National Academy of Sciences of the United States of America · 2020
    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

10 authors at 5 institutions in 4 countries.

Beata Dadacz-NarlochUniversity of Wuerzburg, Institute for Molecular Plant Physiology and Biophysics, D-97082 Wuerzburg, Germany.
Diana Beyhl
Christina Larisch
Enrique J López-Sanjurjo
Ralf Reski
Kazuyuki Kuchitsu
Thomas D Müller
Dirk Becker
Gerald Schönknecht
Rainer Hedrich
University of Würzburg · DEKing Saud University · SAOklahoma State University · USTokyo University of Science · JPUniversity of Freiburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cytosolic calcium homeostasis is pivotal for intracellular signaling and requires sensing of calcium concentrations in the cytosol and accessible stores. Numerous Ca²⁺ binding sites have been characterized in cytosolic proteins. However, little is known about Ca²⁺ binding inside organelles, like the vacuole. The slow vacuolar (SV) channel, encoded by Arabidopsis thaliana TPC1, is regulated by luminal Ca²⁺. However, the D454/fou2 mutation in TPC1 eliminates vacuolar calcium sensitivity and increases store calcium content. In a search for the luminal calcium binding site, structure modeling indicated a possible coordination site formed by residues Glu-450, Asp-454, Glu-456, and Glu-457 on the luminal side of TPC1. Each Glu residue was replaced by Gln, the modified genes were transiently expressed in loss-of-TPC1-function protoplasts, and SV channel responses to luminal calcium were recorded by patch clamp. SV channels lacking any of the four negatively charged residues appeared altered in calcium sensitivity of channel gating. Our results indicate that Glu-450 and Asp-454 are directly involved in Ca²⁺ binding, whereas Glu-456 and Glu-457 are probably involved in connecting the luminal Ca²⁺ binding site to the channel gate. This novel vacuolar calcium binding site represents a potential tool to address calcium storage in plants.

Indexed as

Amino Acid SequenceAnimalsArabidopsisArabidopsis ProteinsBinding SitesCalciumCalcium ChannelsCalcium SignalingHomeostasisHumansIon Channel GatingModels, MolecularModels, TheoreticalMutagenesis, Site-DirectedPatch-Clamp TechniquesProtein ConformationArabidopsis ProteinsCalciumCalcium ChannelsTPC1 protein, ArabidopsisTwo-Pore Channels

Identifiers

PMID21764990
PMCPMC3226227
OpenAlexW2140143197

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.