Evidence map›Paper›PMID 21455789›Full record

ArticlePlant cell reports2011

Arabidopsis MAP kinase phosphatase 1 is phosphorylated and activated by its substrate AtMPK6.

Hyeong Cheol Park, Eun Hyeon Song, Xuan Canh Nguyen, Kyunghee Lee, Kyung Eun Kim, Ho Soo Kim, Sang Min Lee, Sun Ho Kim, Dong Won Bae, Dae-Jin Yun and 1 more

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Article in Plant cell reports, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

24 citing papers in PubMed, 43 citations in OpenAlex.

  1. Emerging Functions of Protein Tyrosine Phosphatases in Plants.International journal of molecular sciences · 2024
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  10. The Second Site Modifier,The Plant cell · 2019
    Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Nuclear Signaling of Plant MAPKs.Frontiers in plant science · 2018
    Review
  16. Review
  17. Article
  18. Article
  19. Review
  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

11 authors at 1 institution in 1 country.

Hyeong Cheol ParkDivision of Applied Life Science (BK21 Program), Plant Molecular Biology and Biotechnology Research Center, Gyeongsang National University, Jinju, 660-701, Republic of Korea.
Eun Hyeon Song
Xuan Canh Nguyen
Kyunghee Lee
Kyung Eun Kim
Ho Soo Kim
Sang Min Lee
Sun Ho Kim
Dong Won Bae
Dae-Jin Yun
Woo Sik Chung
Gyeongsang National University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Arabidopsis MAP kinase phosphatase 1 (AtMKP1) is a member of the mitogen-activated protein kinase (MPK) phosphatase family, which negatively regulates AtMPKs. We have previously shown that AtMKP1 is regulated by calmodulin (CaM). Here, we examined the phosphorylation of AtMKP1 by its substrate AtMPK6. Intriguingly, AtMKP1 was phosphorylated by AtMPK6, one of AtMKP1 substrates. Four phosphorylation sites were identified by phosphoamino acid analysis, TiO(2) chromatography and mass spectrometric analysis. Site-directed mutation of these residues in AtMKP1 abolished the phosphorylation by AtMPK6. In addition, AtMKP1 interacted with AtMPK6 as demonstrated by the yeast two-hybrid system. Finally, the phosphatase activity of AtMKP1 increased approximately twofold following phosphorylation by AtMPK6. By in-gel kinase assays, we showed that AtMKP1 could be rapidly phosphorylated by AtMPK6 in plants. Our results suggest that the catalytic activity of AtMKP1 in plants can be regulated not only by Ca(2+)/CaM, but also by its physiological substrate, AtMPK6.

Indexed as

ArabidopsisArabidopsis ProteinsMitogen-Activated Protein KinasesMutagenesis, Site-DirectedPhosphorylationProtein Tyrosine PhosphatasesSequence DeletionArabidopsis ProteinsMitogen-Activated Protein KinasesMKP1 protein, ArabidopsisMPK6 protein, ArabidopsisProtein Tyrosine Phosphatases

Identifiers

PMID21455789
OpenAlexW2005000195

What OpenQuestion holds

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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.