Evidence map›Paper›PMID 10759527›Full record

ArticlePlant physiology2000

ATMPK4, an Arabidopsis homolog of mitogen-activated protein kinase, is activated in vitro by AtMEK1 through threonine phosphorylation.

Y Huang, H Li, R Gupta, P C Morris, S Luan, J J Kieber

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In one paragraph

Article in Plant physiology, 2000. 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
3.4field-weighted citation impact, top 7% 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, 143 citations in OpenAlex.

  1. Article
  2. Article
  3. TheInternational journal of molecular sciences · 2022
    Article
  4. S-Nitrosation ofFrontiers in plant science · 2022
    Article
  5. Article
  6. Review
  7. PoplarInternational journal of molecular sciences · 2020
    Article
  8. Review
  9. Mitogen-activated protein kinases MPK4 and MPK12 are key components mediating COThe Plant journal : for cell and molecular biology · 2018
    Article
  10. Review
  11. Review
  12. New functions of an old kinase MPK4 in guard cells.Plant signaling & behavior · 2018
    Article
  13. Article
  14. Article
  15. 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

6 authors at 3 institutions in 2 countries.

Y HuangDepartment of Biological Sciences, Laboratory for Molecular Biology, University of Illinois at Chicago, Chicago, Illinois 60607, USA.
H Li
R Gupta
P C Morris
S Luan
J J Kieber
University of Illinois Chicago · USUniversity of California, Berkeley · USHeriot-Watt University · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The modulation of mitogen-activated protein kinase (MAPK) activity regulates many intracellular signaling processes. In animal and yeast cells, MAP kinases are activated via phosphorylation by the dual-specificity kinase MEK (MAP kinase kinase). Several plant homologs of MEK and MAPK have been identified, but the biochemical events underlying the activation of plant MAPKs remain unknown. We describe the in vitro activation of an Arabidopsis homolog of MAP kinase, ATMPK4. ATMPK4 was phosphorylated in vitro by an Arabidopsis MEK homolog, AtMEK1. This phosphorylation occurred principally on threonine (Thr) residues and resulted in elevated ATMPK4 kinase activity. A second Arabidopsis MEK isoform, ATMAP2Kalpha, failed to phosphorylate ATMPK4 in vitro. Tyr dephosphorylation by the Arabidopsis Tyr-specific phosphatase AtPTP1 resulted in an almost complete loss of ATMPK4 activity. Immunoprecipitates of Arabidopsis extracts with anti-ATMPK4 antibodies displayed myelin basic protein kinase activity that was sensitive to treatment with AtPTP1. These results demonstrate that a plant MEK can phosphorylate and activate MAPK, and that Tyr phosphorylation is critical for the catalytic activity of MAPK in plants. Surprisingly, in contrast to the animal enzymes, AtMEK1 may not be a dual-specificity kinase but, rather, the required Tyr phosphorylation on ATMPK4 may result from autophosphorylation.

Indexed as

ArabidopsisBase SequenceDNA PrimersEnzyme ActivationMAP Kinase Kinase 1Mitogen-Activated Protein Kinase KinasesMitogen-Activated Protein KinasesPhosphorylationProtein Serine-Threonine KinasesThreonineDNA PrimersMAP Kinase Kinase 1Mitogen-Activated Protein Kinase KinasesMitogen-Activated Protein KinasesProtein Serine-Threonine KinasesThreonineNon-programmatic

Identifiers

PMID10759527
PMCPMC58966
OpenAlexW2150420445

What OpenQuestion holds

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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.