Evidence map›Paper›PMID 16319177›Full record

ArticleMolecular biology of the cell2006

Regulation of N-cadherin dynamics at neuronal contacts by ligand binding and cytoskeletal coupling.

Olivier Thoumine, Mireille Lambert, René-Marc Mège, Daniel Choquet

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
2.3field-weighted citation impact, top 13% 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

37 citing papers in PubMed, 73 citations in OpenAlex.

  1. Review
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  3. Review
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  6. Spatial and temporal organization of cadherin in punctate adherens junctions.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  7. Article
  8. Article
  9. Integration of Cadherin Adhesion and Cytoskeleton atCold Spring Harbor perspectives in biology · 2017
    Review
  10. Epithelial self-healing is recapitulated by a 3D biomimetic E-cadherin junction.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  11. Article
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  16. Two-tiered coupling between flowing actin and immobilized N-cadherin/catenin complexes in neuronal growth cones.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  17. Article
  18. GRIP1 interlinks N-cadherin and AMPA receptors at vesicles to promote combined cargo transport into dendrites.Proceedings of the National Academy of Sciences of the United States of America · 2014
    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

4 authors at 3 institutions in 1 country.

Olivier ThoumineCNRS, UMR 5091, Institut Magendie de Neurosciences, Université Bordeaux 2, 33077 Bordeaux, France. olivier.thoumine@pcs.u-bordeaux2.fr
Mireille Lambert
René-Marc Mège
Daniel Choquet
Sorbonne Université · FRCentre National de la Recherche Scientifique · FRNeurocentre Magendie · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

N-cadherin plays a key role in axonal outgrowth and synaptogenesis, but how neurons initiate and remodel N-cadherin-based adhesions remains unclear. We addressed this issue with a semiartificial system consisting of N-cadherin coated microspheres adhering to cultured neurons transfected for N-cadherin-GFP. Using optical tweezers, we show that growth cones are particularly reactive to N-cadherin coated microspheres, which they capture in a few seconds and drag rearward. Such strong coupling requires an intact connection between N-cadherin receptors and catenins. As they move to the basis of growth cones, microspheres slow down while gradually accumulating N-cadherin-GFP, demonstrating a clear delay between bead coupling to the actin flow and receptor recruitment. Using FRAP and photoactivation, N-cadherin receptors at bead-to-cell contacts were found to continuously recycle, consistently with a model of ligand-receptor reaction not limited by membrane diffusion. The use of N-cadherin-GFP receptors truncated or mutated in specific cytoplasmic regions show that N-cadherin turnover is exquisitely regulated by catenin partners. Turnover rates are considerably lower than those obtained previously in single molecule studies, demonstrating an active regulation of cadherin bond kinetics in intact cells. Finally, spontaneous neuronal contacts enriched in N-cadherin exhibited similar turnover rates, suggesting that such dynamics of N-cadherin may represent an intrinsic mechanism underlying the plasticity of neuronal adhesions.

Indexed as

Actin CytoskeletonActinsAnimalsCadherinsCateninsCell AdhesionChickensGreen Fluorescent ProteinsGrowth ConesKineticsLigandsMiceMicrospheresModels, BiologicalNeurogliaNeuronsActinsCadherinsCateninsGreen Fluorescent ProteinsLigandsRecombinant Fusion Proteins

Identifiers

PMID16319177
PMCPMC1356595
OpenAlexW2116470668

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.