Evidence map›Paper›PMID 27920157›Full record

ArticlePlant physiology2017

Two SERK Receptor-Like Kinases Interact with EMS1 to Control Anther Cell Fate Determination.

Zhiyong Li, Yao Wang, Jian Huang, Nagib Ahsan, Gabriel Biener, Joel Paprocki, Jay J Thelen, Valerica Raicu, Dazhong Zhao

Open access · bronzeAbstract read
In one paragraph

Article in Plant physiology, 2017. 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
4.5field-weighted citation impact, top 5% 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, 104 citations in OpenAlex.

  1. Article
  2. Review
  3. Ecological Adaptation Mechanisms Underlying Successful Plant Reproduction.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  4. Peptides in plant reproduction-small yet powerful.Frontiers in plant science · 2025
    Review
  5. Review
  6. Review
  7. Article
  8. Bioinformatic and Phenotypic Analysis ofPlants (Basel, Switzerland) · 2024
    Article
  9. DecodingPlants (Basel, Switzerland) · 2024
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. Review
  19. A peptide-mediated, multilateral molecular dialogue for the coordination of pollen wall formation.Proceedings of the National Academy of Sciences of the United States of America · 2022
    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

9 authors at 1 institution in 1 country.

Zhiyong LiDepartment of Biological Sciences (Z.L., Y.W., J.H., V.R., D.Z.) and Department of Physics (G.B., J.P., V.R.), University of Wisconsin, Milwaukee, Wisconsin 53211; and.ORCID 0000-0002-2151-5535
Yao WangDepartment of Biological Sciences (Z.L., Y.W., J.H., V.R., D.Z.) and Department of Physics (G.B., J.P., V.R.), University of Wisconsin, Milwaukee, Wisconsin 53211; and.
Jian HuangDepartment of Biological Sciences (Z.L., Y.W., J.H., V.R., D.Z.) and Department of Physics (G.B., J.P., V.R.), University of Wisconsin, Milwaukee, Wisconsin 53211; and.ORCID 0000-0001-9167-1421
Nagib AhsanDepartment of Biological Sciences (Z.L., Y.W., J.H., V.R., D.Z.) and Department of Physics (G.B., J.P., V.R.), University of Wisconsin, Milwaukee, Wisconsin 53211; and.
Gabriel BienerDepartment of Biological Sciences (Z.L., Y.W., J.H., V.R., D.Z.) and Department of Physics (G.B., J.P., V.R.), University of Wisconsin, Milwaukee, Wisconsin 53211; and.
Joel PaprockiDepartment of Biological Sciences (Z.L., Y.W., J.H., V.R., D.Z.) and Department of Physics (G.B., J.P., V.R.), University of Wisconsin, Milwaukee, Wisconsin 53211; and.
Jay J ThelenDepartment of Biological Sciences (Z.L., Y.W., J.H., V.R., D.Z.) and Department of Physics (G.B., J.P., V.R.), University of Wisconsin, Milwaukee, Wisconsin 53211; and.ORCID 0000-0001-5995-1562
Valerica RaicuDepartment of Biological Sciences (Z.L., Y.W., J.H., V.R., D.Z.) and Department of Physics (G.B., J.P., V.R.), University of Wisconsin, Milwaukee, Wisconsin 53211; and.ORCID 0000-0002-3427-8516
Dazhong ZhaoDepartment of Biological Sciences (Z.L., Y.W., J.H., V.R., D.Z.) and Department of Physics (G.B., J.P., V.R.), University of Wisconsin, Milwaukee, Wisconsin 53211; and dzhao@uwm.edu.ORCID 0000-0002-2045-0717
University of Wisconsin–Milwaukee · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cell signaling pathways mediated by leucine-rich repeat receptor-like kinases (LRR-RLKs) are essential for plant growth, development, and defense. The EMS1 (EXCESS MICROSPOROCYTES1) LRR-RLK and its small protein ligand TPD1 (TAPETUM DETERMINANT1) play a fundamental role in somatic and reproductive cell differentiation during early anther development in Arabidopsis (Arabidopsis thaliana). However, it is unclear whether other cell surface molecules serve as coregulators of EMS1. Here, we show that SERK1 (SOMATIC EMBRYOGENESIS RECEPTOR-LIKE KINASE1) and SERK2 LRR-RLKs act redundantly as coregulatory and physical partners of EMS1. The SERK1/2 genes function in the same genetic pathway as EMS1 in anther development. Bimolecular fluorescence complementation, Förster resonance energy transfer, and coimmunoprecipitation approaches revealed that SERK1 interacted biochemically with EMS1. Transphosphorylation of EMS1 by SERK1 enhances EMS1 kinase activity. Among 12 in vitro autophosphorylation and transphosphorylation sites identified by tandem mass spectrometry, seven of them were found to be critical for EMS1 autophosphorylation activity. Furthermore, complementation test results suggest that phosphorylation of EMS1 is required for its function in anther development. Collectively, these data provide genetic and biochemical evidence of the interaction and phosphorylation between SERK1/2 and EMS1 in anther development.

Indexed as

Cell LineageArabidopsisArabidopsis ProteinsEpistasis, GeneticFlowersFluorescenceModels, BiologicalMutationPhosphorylationProtein BindingProtein KinasesProtein Serine-Threonine KinasesArabidopsis ProteinsAt5g07280 protein, ArabidopsisProtein KinasesProtein Serine-Threonine KinasesSERK1 protein, Arabidopsissomatic embryogenesis receptor-like kinase 2, Arabidopsis

Identifiers

PMID27920157
PMCPMC5210720
OpenAlexW2559957254

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.