Evidence map›Paper›PMID 18552232›Full record

ArticlePlant physiology2008

Interactions between the S-domain receptor kinases and AtPUB-ARM E3 ubiquitin ligases suggest a conserved signaling pathway in Arabidopsis.

Marcus A Samuel, Yashwanti Mudgil, Jennifer N Salt, Frédéric Delmas, Shaliny Ramachandran, Andrea Chilelli, Daphne R Goring

Open access · hybridAbstract read
In one paragraph

Article in Plant physiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 96 papers.

0numbers the graph read from it
0cells of the map it votes in
96citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

96 citing papers in PubMed, 174 citations in OpenAlex.

  1. Article
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  8. Review
  9. Wheat E3 ligasePhysiology and molecular biology of plants : an international journal of functional plant biology · 2025
    Article
  10. Ubiquitin LigaseInternational journal of molecular sciences · 2024
    Article
  11. Fine mapping of a major co-localized QTL associated with self-incompatibility identified in two FTAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2024
    Article
  12. Arabidopsis ubiquitin ligase PUB41 positively regulates ABA-mediated seed dormancy and drought response.Physiology and molecular biology of plants : an international journal of functional plant biology · 2024
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. International journal of molecular sciences · 2024
    Article
  19. Article
  20. Article

36 more citing papers are in PubMed but not listed here.

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.

Marcus A SamuelDepartment of Cell and Systems Biology, University of Toronto, Toronto, Ontario, Canada M5S 3B2.
Yashwanti Mudgil
Jennifer N Salt
Frédéric Delmas
Shaliny Ramachandran
Andrea Chilelli
Daphne R Goring
University of Toronto · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Arabidopsis (Arabidopsis thaliana) genome encompasses multiple receptor kinase families with highly variable extracellular domains. Despite their large numbers, the various ligands and the downstream interacting partners for these kinases have been deciphered only for a few members. One such member, the S-receptor kinase, is known to mediate the self-incompatibility (SI) response in Brassica. S-receptor kinase has been shown to interact and phosphorylate a U-box/ARM-repeat-containing E3 ligase, ARC1, which, in turn, acts as a positive regulator of the SI response. In an effort to identify conserved signaling pathways in Arabidopsis, we performed yeast two-hybrid analyses of various S-domain receptor kinase family members with representative Arabidopsis plant U-box/ARM-repeat (AtPUB-ARM) E3 ligases. The kinase domains from S-domain receptor kinases were found to interact with ARM-repeat domains from AtPUB-ARM proteins. These kinase domains, along with M-locus protein kinase, a positive regulator of SI response, were also able to phosphorylate the ARM-repeat domains in in vitro phosphorylation assays. Subcellular localization patterns were investigated using transient expression assays in tobacco (Nicotiana tabacum) BY-2 cells and changes were detected in the presence of interacting kinases. Finally, potential links to the involvement of these interacting modules to the hormone abscisic acid (ABA) were investigated. Interestingly, AtPUB9 displayed redistribution to the plasma membrane of BY-2 cells when either treated with ABA or coexpressed with the active kinase domain of ARK1. As well, T-DNA insertion mutants for ARK1 and AtPUB9 lines were altered in their ABA sensitivity during germination and acted at or upstream of ABI3, indicating potential involvement of these proteins in ABA responses.

Indexed as

Signal TransductionAbscisic AcidArabidopsisArabidopsis ProteinsCell MembraneCells, CulturedGerminationNicotianaPhosphorylationPlant Growth RegulatorsPlants, Genetically ModifiedProtein KinasesProtein Structure, TertiarySeedsTwo-Hybrid System TechniquesUbiquitin-Protein LigasesAbscisic AcidArabidopsis ProteinsPlant Growth RegulatorsProtein KinasesUbiquitin-Protein Ligases

Identifiers

PMID18552232
PMCPMC2492606
OpenAlexW2131750171

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.