Evidence map›Paper›PMID 16905656›Full record

ArticleThe Plant cell2006

Tobacco WLIM1 is a novel F-actin binding protein involved in actin cytoskeleton remodeling.

Clément Thomas, Céline Hoffmann, Monika Dieterle, Marleen Van Troys, Christophe Ampe, André Steinmetz

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

51 citing papers in PubMed, 91 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. LIM domain proteins in cell mechanobiology.Cytoskeleton (Hoboken, N.J.) · 2021
    Review
  11. Genome-wide identification, characterization and expression analysis of the LIM transcription factor family in quinoa.Physiology and molecular biology of plants : an international journal of functional plant biology · 2021
    Article
  12. Article
  13. Article
  14. Review
  15. Genome-Wide Analysis ofInternational journal of molecular sciences · 2019
    Article
  16. Actin Bundles in The Pollen Tube.International journal of molecular sciences · 2018
    Review
  17. Article
  18. Article
  19. Review
  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

6 authors at 4 institutions in 3 countries.

Clément ThomasCentre de Recherche Public-Santé, L-1526 Luxembourg.
Céline Hoffmann
Monika Dieterle
Marleen Van Troys
Christophe Ampe
André Steinmetz
Laboratoire National de Santé · LUGhent University · BEInstitut de Biologie Moléculaire des Plantes · FRVlaams Instituut voor Biotechnologie · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We used confocal microscopy and in vitro analyses to show that Nicotiana tabacum WLIM1, a LIM domain protein related to animal Cys-rich proteins, is a novel actin binding protein in plants. Green fluorescent protein (GFP)-tagged WLIM1 protein accumulated in the nucleus and cytoplasm of tobacco BY2 cells. It associated predominantly with actin cytoskeleton, as demonstrated by colabeling and treatment with actin-depolymerizing latrunculin B. High-speed cosedimentation assays revealed the ability of WLIM1 to bind directly to actin filaments with high affinity. Fluorescence recovery after photobleaching and fluorescence loss in photobleaching showed a highly dynamic in vivo interaction of WLIM1-GFP with actin filaments. Expression of WLIM1-GFP in BY2 cells significantly delayed depolymerization of the actin cytoskeleton induced by latrunculin B treatment. WLIM1 also stabilized actin filaments in vitro. Importantly, expression of WLIM1-GFP in Nicotiana benthamiana leaves induces significant changes in actin cytoskeleton organization, specifically, fewer and thicker actin bundles than in control cells, suggesting that WLIM1 functions as an actin bundling protein. This hypothesis was confirmed by low-speed cosedimentation assays and direct observation of F-actin bundles that formed in vitro in the presence of WLIM1. Taken together, these data identify WLIM1 as a novel actin binding protein that increases actin cytoskeleton stability by promoting bundling of actin filaments.

Indexed as

Actin CytoskeletonActinsBridged Bicyclo Compounds, HeterocyclicCells, CulturedDinitrobenzenesEscherichia coliGreen Fluorescent ProteinsMicrofilament ProteinsMolecular Sequence DataNicotianaPlant LeavesPlant ProteinsProtein Structure, TertiaryRecombinant Fusion ProteinsSulfanilamidesThiazolesActinsBridged Bicyclo Compounds, HeterocyclicDinitrobenzenesGreen Fluorescent Proteinslatrunculin BMicrofilament ProteinsoryzalinPlant ProteinsRecombinant Fusion ProteinsSulfanilamidesThiazolesThiazolidinesTubulin Modulators

Identifiers

PMID16905656
PMCPMC1560925
OpenAlexW2122195365

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.