Evidence map›Paper›PMID 39361658›Full record

ArticlePlant physiology2024

Calcium-dependent protein kinases 5 and 13 enhance salt tolerance in rice by directly activating OsMPK3/6 kinases.

Shiqi Su, Yimin Jiang, Xiang Zhu, Shibo Yu, Fuxiang Wang, Li Xue, Haitao Cui

Abstract read
In one paragraph

Article in Plant physiology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
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  5. Review
  6. Article
  7. Article
  8. Loss of calcium-dependent protein kinases OsCPK5 and OsCPK13 leads to NLR-dependent resistance in rice.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
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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.

Shiqi SuKey Laboratory of Ministry of Education for Genetics, Breeding and Multiple Utilization of Crops, Fujian University Key Laboratory for Plant-Microbe Interaction, Plant Immunity Center, Fujian Agriculture and Forestry University, Fuzhou 350002, China.
Yimin JiangKey Laboratory of Ministry of Education for Genetics, Breeding and Multiple Utilization of Crops, Fujian University Key Laboratory for Plant-Microbe Interaction, Plant Immunity Center, Fujian Agriculture and Forestry University, Fuzhou 350002, China.
Xiang ZhuKey Laboratory of Ministry of Education for Genetics, Breeding and Multiple Utilization of Crops, Fujian University Key Laboratory for Plant-Microbe Interaction, Plant Immunity Center, Fujian Agriculture and Forestry University, Fuzhou 350002, China.
Shibo YuKey Laboratory of Ministry of Education for Genetics, Breeding and Multiple Utilization of Crops, Fujian University Key Laboratory for Plant-Microbe Interaction, Plant Immunity Center, Fujian Agriculture and Forestry University, Fuzhou 350002, China.
Fuxiang WangKey Laboratory of Ministry of Education for Genetics, Breeding and Multiple Utilization of Crops, Fujian University Key Laboratory for Plant-Microbe Interaction, Plant Immunity Center, Fujian Agriculture and Forestry University, Fuzhou 350002, China.
Li XueCollege of Life Science, Shandong Agricultural University, Tai'an, Shandong 271018, China.
Haitao CuiKey Laboratory of Ministry of Education for Genetics, Breeding and Multiple Utilization of Crops, Fujian University Key Laboratory for Plant-Microbe Interaction, Plant Immunity Center, Fujian Agriculture and Forestry University, Fuzhou 350002, China.ORCID 0000-0002-6343-1014

Funding

German Research Foundation M-0275National Natural Science Foundation of China 31970281Natural Science Foundation 2023J02011Scientific Research Foundation of Graduate School of Fujian Agriculture and Forestry University 324-1122yb083
6 · The paper itself

Abstract

Mitogen-activated protein kinases (MAPKs/MPKs) are pivotal regulators in many stress-signaling pathways in plants. The dual phosphorylation of the TXY motif by MAP kinase kinases (MKKs) is essential for activating MAPKs. Here, we reveal a mechanism for MAPK activation that bypasses the need for MKKs. We identified rice (Oryza sativa) calcium-dependent protein kinase 5 (OsCPK5) and OsCPK13 as positive regulators in salt stress tolerance. These kinases are essential for the full activation of OsMPK3 and OsMPK6 in response to elevated sodium levels, with both OsMPK3 and OsMPK6 also acting as positive regulators in rice salt tolerance. Biochemical analysis demonstrated that OsCPK5/13 directly interact with and activate OsMPK3/6 by phosphorylating the TXY motif in vitro and in vivo. Additionally, we have discovered that OsCPK5/13 relocate from the cell membrane to the nucleus in response to salt stress. This process relies on their N-terminal myristoylation and a calcium-dependent phosphorylation event within the N-terminus. Our results elucidate a MAPK activation pathway in rice that is independent of traditional MKK-mediated phosphorylation, highlighting the crucial roles of OsCPK5 and OsCPK13 in directly phosphorylating and activating OsMPK3/6, which are important for rice tolerance to salt stress.

Indexed as

OryzaPlant ProteinsSalt ToleranceGene Expression Regulation, PlantMitogen-Activated Protein Kinase KinasesMitogen-Activated Protein KinasesPhosphorylationMitogen-Activated Protein Kinase KinasesMitogen-Activated Protein KinasesPlant Proteins

Identifiers

PMID39361658
PMCPMC11638333

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Registered trials

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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.