Evidence map›Paper›PMID 24475319›Full record

ArticlePloS one2014

Structural characterization of the mechanosensitive channel candidate MCA2 from Arabidopsis thaliana.

Hideki Shigematsu, Kazuko Iida, Masataka Nakano, Pratima Chaudhuri, Hidetoshi Iida, Kuniaki Nagayama

Abstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Structure, Function, and Applications of Soybean Calcium Transporters.International journal of molecular sciences · 2022
    Review
  6. Article
  7. Review
  8. MCAs in Arabidopsis are CaNature communications · 2021
    Article
  9. Review
  10. Review
  11. PIEZO ion channel is required for root mechanotransduction inProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  12. Article
  13. Calcium Signaling-Mediated Plant Response to Cold Stress.International journal of molecular sciences · 2018
    Review
  14. CaScientific reports · 2018
    Article
  15. Review
  16. Article
  17. Article
  18. Review
  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

6 authors.

Hideki ShigematsuOkazaki Institute for Integrative Bioscience, National Institutes of Natural Sciences, Okazaki, Aichi, Japan.
Kazuko IidaBiomembrane Laboratory, Tokyo Metropolitan Institute of Medical Science, Setagaya-ku, Tokyo, Japan.
Masataka NakanoDepartment of Biology, Tokyo Gakugei University, Koganei, Tokyo, Japan.
Pratima ChaudhuriOkazaki Institute for Integrative Bioscience, National Institutes of Natural Sciences, Okazaki, Aichi, Japan.
Hidetoshi IidaOkazaki Institute for Integrative Bioscience, National Institutes of Natural Sciences, Okazaki, Aichi, Japan ; Department of Biology, Tokyo Gakugei University, Koganei, Tokyo, Japan.
Kuniaki NagayamaOkazaki Institute for Integrative Bioscience, National Institutes of Natural Sciences, Okazaki, Aichi, Japan ; National Institute for Physiological Sciences, National Institutes of Natural Sciences, Okazaki, Aichi, Japan ; Department of Physiological Sciences, Graduate University for Advanced Studies, Okazaki, Aichi, Japan.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mechanosensing in plants is thought to be governed by sensory complexes containing a Ca²⁺-permeable, mechanosensitive channel. The plasma membrane protein MCA1 and its paralog MCA2 from Arabidopsis thaliana are involved in mechanical stress-induced Ca²⁺ influx and are thus considered as candidates for such channels or their regulators. Both MCA1 and MCA2 were functionally expressed in Sf9 cells using a baculovirus system in order to elucidate their molecular natures. Because of the abundance of protein in these cells, MCA2 was chosen for purification. Purified MCA2 in a detergent-solubilized state formed a tetramer, which was confirmed by chemical cross-linking. Single-particle analysis of cryo-electron microscope images was performed to depict the overall shape of the purified protein. The three-dimensional structure of MCA2 was reconstructed at a resolution of 26 Å from 5,500 particles and appears to comprise a small transmembrane region and large cytoplasmic region.

Indexed as

Models, MolecularAnimalsArabidopsisArabidopsis ProteinsCalcium ChannelsCryoelectron MicroscopyMechanotransduction, CellularMembrane ProteinsProtein ConformationSaccharomyces cerevisiaeSf9 CellsSpodopteraArabidopsis ProteinsCalcium ChannelsMCA1 protein, ArabidopsisMCA2 protein, ArabidopsisMembrane Proteins

Identifiers

PMID24475319
PMCPMC3903776

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.