Evidence map›Paper›PMID 24368786›Full record

ArticleThe Plant cell2013

Calcium/Calmodulin-dependent protein kinase is negatively and positively regulated by calcium, providing a mechanism for decoding calcium responses during symbiosis signaling.

J Benjamin Miller, Amitesh Pratap, Akira Miyahara, Liang Zhou, Stephen Bornemann, Richard J Morris, Giles E D Oldroyd

Open access · hybridAbstract read
In one paragraph

Article in The Plant cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
18.5field-weighted citation impact, top 1% 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

52 citing papers in PubMed, 145 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Differential Responses ofPlants (Basel, Switzerland) · 2023
    Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Review
  12. Molecular Regulation of Arbuscular Mycorrhizal Symbiosis.International journal of molecular sciences · 2022
    Review
  13. Article
  14. Review
  15. Article
  16. Review
  17. Identification of differentially expressed genes associated with aluminum resistance in the soybean plant.Physiology and molecular biology of plants : an international journal of functional plant biology · 2021
    Article
  18. Article
  19. Article
  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

7 authors at 1 institution in 1 country.

J Benjamin MillerJohn Ines Centre, Norwich NR4 7UH, United Kingdom.
Amitesh Pratap
Akira Miyahara
Liang Zhou
Stephen Bornemann
Richard J Morris
Giles E D Oldroyd
John Innes Centre · GB

Funding

Biotechnology and Biological Sciences Research Council BB/F017294/1Biotechnology and Biological Sciences Research Council BB/J004553/1Biotechnology and Biological Sciences Research Council BBS/E/J/00000603Biotechnology and Biological Sciences Research Council BBS/E/J/00000611Biotechnology and Biological Sciences Research Council BBS/E/J/000C0631Biotechnology and Biological Sciences Research Council BBS/E/J/000CA336
6 · The paper itself

Abstract

The establishment of symbiotic associations in plants requires calcium oscillations that must be decoded to invoke downstream developmental programs. In animal systems, comparable calcium oscillations are decoded by calmodulin (CaM)-dependent protein kinases, but symbiotic signaling involves a calcium/CaM-dependent protein kinase (CCaMK) that is unique to plants. CCaMK differs from the animal CaM kinases by its dual ability to bind free calcium, via calcium binding EF-hand domains on the protein, or to bind calcium complexed with CaM, via a CaM binding domain. In this study, we dissect this dual regulation of CCaMK by calcium. We find that calcium binding to the EF-hand domains promotes autophosphorylation, which negatively regulates CCaMK by stabilizing the inactive state of the protein. By contrast, calcium-dependent CaM binding overrides the effects of autophosphorylation and activates the protein. The differential calcium binding affinities of the EF-hand domains compared with those of CaM suggest that CCaMK is maintained in the inactive state at basal calcium concentrations and is activated via CaM binding during calcium oscillations. This work provides a model for decoding calcium oscillations that uses differential calcium binding affinities to create a robust molecular switch that is responsive to calcium concentrations associated with both the basal state and with oscillations.

Indexed as

Calcium SignalingSymbiosisCalciumCalcium-Calmodulin-Dependent Protein KinasesMedicago truncatulaModels, BiologicalModels, MolecularMolecular Sequence DataPhosphorylationProtein Structure, TertiarySinorhizobium melilotiCalciumCalcium-Calmodulin-Dependent Protein Kinases

Identifiers

PMID24368786
PMCPMC3904005
OpenAlexW2155012764

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.