Evidence map›Paper›PMID 26784444›Full record

ArticlePloS one2016

Analysis of Phosphorylation of the Receptor-Like Protein Kinase HAESA during Arabidopsis Floral Abscission.

Isaiah Taylor, Ying Wang, Kati Seitz, John Baer, Stefan Bennewitz, Brian P Mooney, John C Walker

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
6.9field-weighted citation impact, top 4% 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

21 citing papers in PubMed, 41 citations in OpenAlex.

  1. Review
  2. Chimerolectins: Classification, structural architecture, and functional perspectives.Protein science : a publication of the Protein Society · 2025
    Review
  3. Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Targeted Profiling of Protein Phosphorylation in Plants.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  10. Article
  11. Activation loop phosphorylation of a non-RD receptor kinase initiates plant innate immune signaling.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  12. Review
  13. Regulation of Three Key Kinases of Brassinosteroid Signaling Pathway.International journal of molecular sciences · 2020
    Review
  14. Review
  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

7 authors at 1 institution in 1 country.

Isaiah TaylorDivision of Biological Science, University of Missouri, Columbia, Missouri, United States of America.
Ying WangDivision of Biological Science, University of Missouri, Columbia, Missouri, United States of America.
Kati SeitzDivision of Biological Science, University of Missouri, Columbia, Missouri, United States of America.
John BaerDivision of Biological Science, University of Missouri, Columbia, Missouri, United States of America.
Stefan BennewitzDivision of Biological Science, University of Missouri, Columbia, Missouri, United States of America.
Brian P MooneyInterdisciplinary Plant Group, University of Missouri, Columbia, Missouri, United States of America.
John C WalkerDivision of Biological Science, University of Missouri, Columbia, Missouri, United States of America.
University of Missouri · US

Funding

MOLECULAR BASIS OF GENE EXPRESSION AND SIGNAL PROCESSINGT32GM008396 · NIGMS · UNIVERSITY OF MISSOURI-COLUMBIA · PI HANNINK, MARK · 1991 to 2021
$4.1M
NIGMS NIH HHS 5T32GM008396NIGMS NIH HHS T32 GM008396
6 · The paper itself

Abstract

Receptor-like protein kinases (RLKs) are the largest family of plant transmembrane signaling proteins. Here we present functional analysis of HAESA, an RLK that regulates floral organ abscission in Arabidopsis. Through in vitro and in vivo analysis of HAE phosphorylation, we provide evidence that a conserved phosphorylation site on a region of the HAE protein kinase domain known as the activation segment positively regulates HAE activity. Additional analysis has identified another putative activation segment phosphorylation site common to multiple RLKs that potentially modulates HAE activity. Comparative analysis suggests that phosphorylation of this second activation segment residue is an RLK specific adaptation that may regulate protein kinase activity and substrate specificity. A growing number of RLKs have been shown to exhibit biologically relevant dual specificity toward serine/threonine and tyrosine residues, but the mechanisms underlying dual specificity of RLKs are not well understood. We show that a phospho-mimetic mutant of both HAE activation segment residues exhibits enhanced tyrosine auto-phosphorylation in vitro, indicating phosphorylation of this residue may contribute to dual specificity of HAE. These results add to an emerging framework for understanding the mechanisms and evolution of regulation of RLK activity and substrate specificity.

Indexed as

ArabidopsisArabidopsis ProteinsCatalytic DomainFlowersGene Expression Regulation, PlantModels, MolecularMutationPhosphorylationProtein Serine-Threonine KinasesSubstrate SpecificityTyrosineArabidopsis ProteinsProtein Serine-Threonine KinasesRLK5 protein, ArabidopsisTyrosine

Identifiers

PMID26784444
PMCPMC4718614
OpenAlexW2395962300

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.