Evidence map›Paper›PMID 25172143›Full record

ArticleThe Plant cell2014

Manipulation of mitogen-activated protein kinase kinase signaling in the Arabidopsis stomatal lineage reveals motifs that contribute to protein localization and signaling specificity.

Gregory R Lampard, Diego L Wengier, Dominique C Bergmann

Erratum issuedOpen access · hybridAbstract 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. An erratum has been issued. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

19 citing papers in PubMed, 34 citations in OpenAlex.

  1. Clathrin-mediated endocytosis of ERECTA family receptors is essential for proper stomatal development inProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
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  6. Review
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  8. Review
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  10. Review
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  12. Stomatal Development and Perspectives toward Agricultural Improvement.Cold Spring Harbor perspectives in biology · 2019
    Review
  13. Article
  14. Article
  15. Article
  16. Molecular control of stomatal development.The Biochemical journal · 2018
    Review
  17. Article
  18. Article
  19. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 2 institutions in 1 country.

Gregory R LampardHoward Hughes Medical Institute, Stanford University, Stanford, California 94305-5020.
Diego L WengierHoward Hughes Medical Institute, Stanford University, Stanford, California 94305-5020.
Dominique C BergmannHoward Hughes Medical Institute, Stanford University, Stanford, California 94305-5020 Department of Biology, Stanford University, Stanford, California 94305-5020 dbergmann@stanford.edu.
Stanford University · USHoward Hughes Medical Institute · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

When multiple mitogen-activated protein kinase (MAPK) components are recruited recurrently to transduce signals of different origins, and often opposing outcomes, mechanisms to enforce signaling specificity are of utmost importance. These mechanisms are largely uncharacterized in plant MAPK signaling networks. The Arabidopsis thaliana stomatal lineage was previously used to show that when rendered constitutively active, four MAPK kinases (MKKs), MKK4/5/7/9, are capable of perturbing stomatal development and that these kinases comprise two pairs, MKK4/5 and MKK7/9, with both overlapping and divergent functions. We characterized the contributions of specific structural domains of these four "stomatal" MKKs to MAPK signaling output and specificity both in vitro and in vivo within the three discrete cell types of the stomatal lineage. These results verify the influence of functional docking (D) domains of MKKs on MAPK signal output and identify novel regulatory functions for previously uncharacterized structures within the N termini of MKK4/5. Beyond this, we present a novel function of the D-domains of MKK7/9 in regulating the subcellular localization of these kinases. These results provide tools to broadly assess the extent to which these and additional motifs within MKKs function to regulate MAPK signal output throughout the plant.

Indexed as

MAP Kinase Signaling SystemAmino Acid SequenceArabidopsisArabidopsis ProteinsBinding SitesGene DeletionMAP Kinase Kinase 7Mitogen-Activated Protein Kinase KinasesMitogen-Activated Protein KinasesMolecular Sequence DataPlant StomataProtein Structure, TertiaryProtein TransportSequence AlignmentArabidopsis ProteinsBUD1 protein, ArabidopsisMAP Kinase Kinase 7Mitogen-Activated Protein Kinase KinasesMitogen-Activated Protein KinasesMKK4 protein, ArabidopsisMKK5 protein, ArabidopsisMKK9 protein, Arabidopsis

Identifiers

PMID25172143
PMCPMC4371834
OpenAlexW2129073342

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.