Evidence map›Paper›PMID 36869735›Full record

ArticleJournal of experimental botany2023

A point mutation in the kinase domain of CRK10 leads to xylem vessel collapse and activation of defence responses in Arabidopsis.

Maiara Piovesana, Ana K M Wood, Daniel P Smith, Michael J Deery, Richard Bayliss, Esther Carrera, Nikolaus Wellner, Ondrej Kosik, Johnathan A Napier, Smita Kurup and 1 more

Open access · hybridAbstract read
In one paragraph

Article in Journal of experimental botany, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
16.7field-weighted citation impact, top 1% 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

9 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. 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 6 institutions in 2 countries.

Maiara PiovesanaDepartment of Plant Sciences, Rothamsted Research, Harpenden AL5 2JQ, UK.
Ana K M WoodDepartment of Biointeractions and Crop Protection, Rothamsted Research, Harpenden AL5 2JQ, UK.
Daniel P SmithDepartment of Computational and Analytical Sciences, Rothamsted Research, Harpenden AL5 2JQ, UK.
Michael J DeeryCambridge Centre for Proteomics, University of Cambridge, Cambridge CB2 1QR, UK.
Richard BaylissSchool of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, UK.ORCID 0000-0003-0604-2773
Esther CarreraInstituto de Biología Molecular y Celular de Plantas, Universidad Politècnica de València, Valencia 46022, Spain.
Nikolaus WellnerQuadram Institute, Norwich Research Park, Norwich NR4 7UQ, UK.
Ondrej KosikDepartment of Plant Sciences, Rothamsted Research, Harpenden AL5 2JQ, UK.
Johnathan A NapierDepartment of Plant Sciences, Rothamsted Research, Harpenden AL5 2JQ, UK.
Smita KurupDepartment of Plant Sciences, Rothamsted Research, Harpenden AL5 2JQ, UK.
Michaela C MatthesDepartment of Plant Sciences, Rothamsted Research, Harpenden AL5 2JQ, UK.ORCID 0000-0001-8475-2901
Rothamsted Research · GBInstituto de Biología Molecular y Celular de Plantas · ESNorwich Research Park · GBUniversity of Cambridge · GBUniversity of Exeter · GBUniversity of Leeds · GB

Funding

Biotechnology and Biological Sciences Research Council BBS/E/C/000I0420
6 · The paper itself

Abstract

Cysteine-rich receptor-like kinases (CRKs) are a large family of plasma membrane-bound receptors ubiquitous in higher plants. However, despite their prominence, their biological roles have remained largely elusive so far. In this study we report the characterization of an Arabidopsis mutant named crk10-A397T in which alanine 397 has been replaced by a threonine in the αC helix of the kinase domain of CRK10, known to be a crucial regulatory module in mammalian kinases. The crk10-A397T mutant is a dwarf that displays collapsed xylem vessels in the root and hypocotyl, whereas the vasculature of the inflorescence develops normally. In situ phosphorylation assays with His-tagged wild type and crk10-A397T versions of the CRK10 kinase domain revealed that both alleles are active kinases capable of autophosphorylation, with the newly introduced threonine acting as an additional phosphorylation site in crk10-A397T. Transcriptomic analysis of wild type and crk10-A397T mutant hypocotyls revealed that biotic and abiotic stress-responsive genes are constitutively up-regulated in the mutant, and a root-infection assay with the vascular pathogen Fusarium oxysporum demonstrated that the mutant has enhanced resistance to this pathogen compared with wild type plants. Taken together our results suggest that crk10-A397T is a gain-of-function allele of CRK10, the first such mutant to have been identified for a CRK in Arabidopsis.

Indexed as

ArabidopsisArabidopsis ProteinsGene Expression Regulation, PlantPoint MutationProtein KinasesProtein Serine-Threonine KinasesArabidopsis ProteinsProtein KinasesProtein Serine-Threonine KinasesArabidopsiscysteine-rich receptor-like kinase CRK10defence responseFusarium oxysporumgain-of-function mutationkinase regulationtranscriptomicsxylem vessel collapseαC helix

Identifiers

PMID36869735
PMCPMC10199123
OpenAlexW4323066580

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.