Evidence map›Paper›PMID 25284001›Full record

ArticleThe Plant journal : for cell and molecular biology2015

Probing formation of cargo/importin-α transport complexes in plant cells using a pathogen effector.

Lennart Wirthmueller, Charlotte Roth, Georgina Fabro, Marie-Cécile Caillaud, Ghanasyam Rallapalli, Shuta Asai, Jan Sklenar, Alexandra M E Jones, Marcel Wiermer, Jonathan D G Jones and 1 more

Open access · hybridAbstract read
In one paragraph

Article in The Plant journal : for cell and molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

19 citing papers in PubMed, 53 citations in OpenAlex.

  1. Article
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  4. Review
  5. Review
  6. Exploiting breakdown in nonhost effector-target interactions to boost host disease resistance.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. MOS6 and TN13 in plant immunity.Plant signaling & behavior · 2018
    Article
  17. Nuclear Import ofFrontiers in plant science · 2018
    Article
  18. Article
  19. 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 4 institutions in 2 countries.

Lennart WirthmuellerThe Sainsbury Laboratory, Norwich Research Park, Norwich, NR4 7UH, UK; Department of Biological Chemistry, John Innes Centre, Norwich Research Park, Norwich, NR4 7UH, UK.
Charlotte Roth
Georgina Fabro
Marie-Cécile Caillaud
Ghanasyam Rallapalli
Shuta Asai
Jan Sklenar
Alexandra M E Jones
Marcel Wiermer
Jonathan D G Jones
Mark J Banfield
Sainsbury Laboratory · GBNorwich Research Park · GBUniversity of Göttingen · DEJohn Innes Centre · GB

Funding

Biotechnology and Biological Sciences Research Council BBJ00453Biotechnology and Biological Sciences Research Council BBK009176Biotechnology and Biological Sciences Research Council BB/K009176/1Biotechnology and Biological Sciences Research Council BBS/E/J/000C0624
6 · The paper itself

Abstract

Importin-αs are essential adapter proteins that recruit cytoplasmic proteins destined for active nuclear import to the nuclear transport machinery. Cargo proteins interact with the importin-α armadillo repeat domain via nuclear localization sequences (NLSs), short amino acids motifs enriched in Lys and Arg residues. Plant genomes typically encode several importin-α paralogs that can have both specific and partially redundant functions. Although some cargos are preferentially imported by a distinct importin-α it remains unknown how this specificity is generated and to what extent cargos compete for binding to nuclear transport receptors. Here we report that the effector protein HaRxL106 from the oomycete pathogen Hyaloperonospora arabidopsidis co-opts the host cell's nuclear import machinery. We use HaRxL106 as a probe to determine redundant and specific functions of importin-α paralogs from Arabidopsis thaliana. A crystal structure of the importin-α3/MOS6 armadillo repeat domain suggests that five of the six Arabidopsis importin-αs expressed in rosette leaves have an almost identical NLS-binding site. Comparison of the importin-α binding affinities of HaRxL106 and other cargos in vitro and in plant cells suggests that relatively small affinity differences in vitro affect the rate of transport complex formation in vivo. Our results suggest that cargo affinity for importin-α, sequence variation at the importin-α NLS-binding sites and tissue-specific expression levels of importin-αs determine formation of cargo/importin-α transport complexes in plant cells.

Indexed as

Active Transport, Cell NucleusAmino Acid SequenceArabidopsisArabidopsis ProteinsConserved SequenceEscherichia coliHost-Pathogen InteractionsKaryopherinsModels, MolecularOomycetesProtein Structure, TertiaryArabidopsis ProteinsKaryopherinsMOS6 protein, ArabidopsisArabidopsis thalianaHyaloperonospora arabidopsidisimportin-αnuclear localization sequencenucleo-cytoplasmic transportoomycete effectorplant innate immunity

Identifiers

PMID25284001
PMCPMC4350430
OpenAlexW2088366790

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.