Evidence map›Paper›PMID 20442373›Full record

ArticleThe Plant cell2010

Alteration of substrate specificity: the variable N-terminal domain of tobacco Ca(2+)-dependent protein kinase is important for substrate recognition.

Takeshi Ito, Masaru Nakata, Jutarou Fukazawa, Sarahmi Ishida, Yohsuke Takahashi

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
11.6field-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

46 citing papers in PubMed, 97 citations in OpenAlex.

  1. Article
  2. Research Progress onBiology · 2025
    Review
  3. Article
  4. Calcium signaling-mediated transcriptional reprogramming during abiotic stress response in plants.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2023
    Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Calcium-Dependent Protein Kinases in Phytohormone Signaling Pathways.International journal of molecular sciences · 2017
    Review
  16. Article
  17. 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

5 authors at 3 institutions in 1 country.

Takeshi ItoDepartment of Biological Science, Graduate School of Science, Hiroshima University, Kagamiyama, Higashi-Hiroshima, Japan.
Masaru Nakata
Jutarou Fukazawa
Sarahmi Ishida
Yohsuke Takahashi
Hiroshima University · JPRIKEN Center for Sustainable Resource Science · JPThe University of Tokyo · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein kinases are major signaling molecules that are involved in a variety of cellular processes. However, the molecular mechanisms whereby protein kinases discriminate specific substrates are still largely unknown. Ca(2+)-dependent protein kinases (CDPKs) play central roles in Ca(2+) signaling in plants. Previously, we found that a tobacco (Nicotiana tabacum) CDPK1 negatively regulated the transcription factor REPRESSION OF SHOOT GROWTH (RSG), which is involved in gibberellin feedback regulation. Here, we found that the variable N-terminal domain of CDPK1 is necessary for the recognition of RSG. A mutation (R10A) in the variable N-terminal domain of CDPK1 reduced both RSG binding and RSG phosphorylation while leaving kinase activity intact. Furthermore, the R10A mutation suppressed the in vivo function of CDPK1. The substitution of the variable N-terminal domain of an Arabidopsis thaliana CDPK, At CPK9, with that of Nt CDPK1 conferred RSG kinase activities. This chimeric CDPK behaved according to the identity of the variable N-terminal domain in transgenic plants. Our results open the possibility of engineering the substrate specificity of CDPK by manipulation of the variable N-terminal domain, enabling a rational rewiring of cellular signaling pathways.

Indexed as

Amino Acid SubstitutionArabidopsisArabidopsis ProteinsArginineBasic-Leucine Zipper Transcription FactorsCalciumCalcium-Binding ProteinsCalcium-Calmodulin-Dependent Protein KinasesMolecular Sequence DataMutationNicotianaPlant ProteinsProtein BindingProtein KinasesProtein Structure, TertiaryRepressor ProteinsArabidopsis ProteinsArginineATCDPK1 protein, ArabidopsisBasic-Leucine Zipper Transcription FactorsCalciumCalcium-Binding ProteinsCalcium-Calmodulin-Dependent Protein KinasesPlant ProteinsProtein KinasesRepressor ProteinsRSG protein, Nicotiana tabacum

Identifiers

PMID20442373
PMCPMC2899867
OpenAlexW2106229596

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.