Evidence map›Paper›PMID 25035404›Full record

ArticleThe Plant cell2014

Direct phosphorylation and activation of a mitogen-activated protein kinase by a calcium-dependent protein kinase in rice.

Kabin Xie, Jianping Chen, Qin Wang, Yinong Yang

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed
11.7field-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

67 citing papers in PubMed, 148 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Article
  6. Calcium signaling in crops.The New phytologist · 2026
    Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. All Roads Lead to Rome: Pathways to Engineering Disease Resistance in Plants.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Transcriptome Regulation Mechanisms Difference between Female and MaleInternational journal of molecular sciences · 2024
    Article
  20. Article

7 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

4 authors at 1 institution in 1 country.

Kabin XieDepartment of Plant Pathology and Environmental Microbiology, The Huck Institutes of the Life Sciences, Pennsylvania State University, University Park, Pennsylvania 16802.ORCID http://orcid.org/0000-0003-0643-2456
Jianping ChenDepartment of Plant Pathology and Environmental Microbiology, The Huck Institutes of the Life Sciences, Pennsylvania State University, University Park, Pennsylvania 16802.
Qin WangDepartment of Plant Pathology and Environmental Microbiology, The Huck Institutes of the Life Sciences, Pennsylvania State University, University Park, Pennsylvania 16802.
Yinong YangDepartment of Plant Pathology and Environmental Microbiology, The Huck Institutes of the Life Sciences, Pennsylvania State University, University Park, Pennsylvania 16802 yuy3@psu.edu.ORCID http://orcid.org/0000-0002-2698-1754
Pennsylvania State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The mitogen-activated protein kinase (MAPK) is a pivotal point of convergence for many signaling pathways in eukaryotes. In the classical MAPK cascade, a signal is transmitted via sequential phosphorylation and activation of MAPK kinase kinase, MAPK kinase (MKK), and MAPK. The activation of MAPK is dependent on dual phosphorylation of a TXY motif by an MKK, which is considered the sole kinase to phosphorylate and activate MAPK. Here, we report a novel regulatory mechanism of MAPK phosphorylation and activation besides the canonical MAPK cascade. A rice (Oryza sativa) calcium-dependent protein kinase (CDPK), CPK18, was identified as an upstream kinase of MAPK (MPK5) in vitro and in vivo. Curiously, CPK18 was shown to phosphorylate and activate MPK5 without affecting the phosphorylation of its TXY motif. Instead, CPK18 was found to predominantly phosphorylate two Thr residues (Thr-14 and Thr-32) that are widely conserved in MAPKs from land plants. Further analyses reveal that the newly identified CPK18-MPK5 pathway represses defense gene expression and negatively regulates rice blast resistance. Our results suggest that land plants have evolved an MKK-independent phosphorylation pathway that directly connects calcium signaling to the MAPK machinery.

Indexed as

Gene Expression Regulation, PlantSignal TransductionAmino Acid SequenceCalciumCalcium-Calmodulin-Dependent Protein KinasesEnzyme ActivationGene Expression Regulation, EnzymologicGenes, ReporterMagnaportheMitogen-Activated Protein Kinase KinasesMitogen-Activated Protein KinasesModels, GeneticMolecular Sequence DataMutationOryzaPhosphorylationCalciumCalcium-Calmodulin-Dependent Protein KinasesMitogen-Activated Protein Kinase KinasesMitogen-Activated Protein KinasesPlant ProteinsProtein KinasesRecombinant Fusion Proteins

Identifiers

PMID25035404
PMCPMC4145133
OpenAlexW2142222966

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.