Evidence map›Paper›PMID 28207053›Full record

ArticleJournal of experimental botany2017

Identification of critical functional residues of receptor-like kinase ERECTA.

Pawel Z Kosentka, Liang Zhang, Yonas A Simon, Binita Satpathy, Richard Maradiaga, Omar Mitoubsi, Elena D Shpak

Open access · greenAbstract read
In one paragraph

Article in Journal of experimental botany, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.8field-weighted citation impact, top 30% 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

14 citing papers in PubMed, 41 citations in OpenAlex.

  1. Review
  2. Preventing inappropriate signals pre- and post-ligand perception by a toggle switch mechanism of ERECTA.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Article
  4. Article
  5. TomatoFrontiers in plant science · 2023
    Article
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  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
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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.

Pawel Z KosentkaDepartment of Biochemistry, Cellular and Molecular Biology, University of Tennessee, Knoxville, TN 37996, USA.
Liang ZhangDepartment of Biochemistry, Cellular and Molecular Biology, University of Tennessee, Knoxville, TN 37996, USA.
Yonas A SimonDepartment of Biochemistry, Cellular and Molecular Biology, University of Tennessee, Knoxville, TN 37996, USA.
Binita SatpathyDepartment of Biochemistry, Cellular and Molecular Biology, University of Tennessee, Knoxville, TN 37996, USA.
Richard MaradiagaDepartment of Biochemistry, Cellular and Molecular Biology, University of Tennessee, Knoxville, TN 37996, USA.
Omar MitoubsiDepartment of Biochemistry, Cellular and Molecular Biology, University of Tennessee, Knoxville, TN 37996, USA.
Elena D ShpakDepartment of Biochemistry, Cellular and Molecular Biology, University of Tennessee, Knoxville, TN 37996, USA.
University of Tennessee at Knoxville · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In plants, extracellular signals are primarily sensed by plasma membrane-localized receptor-like kinases (RLKs). ERECTA is a leucine-rich repeat RLK that together with its paralogs ERECTA-like 1 (ERL1) and ERL2 regulates multiple aspects of plant development. ERECTA forms complexes with a range of co-receptors and senses secreted cysteine-rich small proteins from the EPF/EPFL family. Currently the mechanism of the cytoplasmic domain activation and transmission of the signal by ERECTA is unclear. To gain a better understanding we performed a structure-function analysis by introducing altered ERECTA genes into erecta and erecta erl1 erl2 mutants. These experiments indicated that ERECTA's ability to phosphorylate is functionally significant, and that while the cytoplasmic juxtamembrane domain is important for ERECTA function, the C-terminal tail is not. An analysis of multiple putative phosphorylation sites identified four amino acids in the activation segment of the kinase domain as functionally important. Homology of those residues to functionally significant amino acids in multiple other plant RLKs emphasizes similarities in RLK function. Specifically, our data predicts Thr812 as a primary site of phosphor-activation and potential inhibitory phosphorylation of Tyr815 and Tyr820. In addition, our experiments suggest that there are differences in the molecular mechanism of ERECTA function during regulation of stomata development and in elongation of above-ground organs.

Indexed as

ArabidopsisArabidopsis ProteinsCatalytic DomainGene Expression Regulation, PlantGenes, PlantPhosphorylationPlants, Genetically ModifiedProtein Serine-Threonine KinasesReceptors, Cell SurfaceSequence AlignmentSignal TransductionArabidopsis ProteinsER protein, ArabidopsisProtein Serine-Threonine KinasesReceptors, Cell SurfaceActivation segmentERECTAkinase domainLRR-RLKphosphorylationreceptor kinasesignal transductionsite-directed mutagenesisstructure–functional analysis

Identifiers

PMID28207053
PMCPMC5441908
OpenAlexW2588696102

What OpenQuestion holds

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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.