Evidence map›Paper›PMID 15254265›Full record

ArticleMolecular biology of the cell2004

NrCAM coupling to the cytoskeleton depends on multiple protein domains and partitioning into lipid rafts.

Julien Falk, Olivier Thoumine, Caroline Dequidt, Daniel Choquet, Catherine Faivre-Sarrailh

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
–field-weighted citation impact
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

27 citing papers in PubMed.

  1. Article
  2. CD82 and Gangliosides Tune CD81 Membrane Behavior.International journal of molecular sciences · 2021
    Article
  3. Article
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  7. Review
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  13. Article
  14. Trafficking guidance receptors.Cold Spring Harbor perspectives in biology · 2010
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  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

5 authors.

Julien FalkNeurogenèse et Morphogenèse du Développement à l'Adulte, UMR 6156 CNRS, Institut de Biologie du Développement de Marseille, Marseille, France.
Olivier Thoumine
Caroline Dequidt
Daniel Choquet
Catherine Faivre-Sarrailh

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

NrCAM is a cell adhesion molecule of the L1 family that is implicated in the control of axonal growth. Adhesive contacts may promote advance of the growth cone by triggering the coupling of membrane receptors with the F-actin retrograde flow. We sought to understand the mechanisms leading to clutching the F-actin at the site of ligand-mediated clustering of NrCAM. Using optical tweezers and single particle tracking of beads coated with the ligand TAG-1, we analyzed the mobility of NrCAM-deletion mutants transfected in a neuroblastoma cell line. Deletion of the cytoplasmic tail did not prevent the coupling of NrCAM to the actin flow. An additional deletion of the FNIII domains to remove cis-interactions, was necessary to abolish the rearward movement of TAG-1 beads, which instead switched to a stationary behavior. Next, we showed that the actin-dependent retrograde movement of NrCAM required partitioning into lipid rafts as indicated by cholesterol depletion experiments using methyl-beta-cyclodextrin. Recruitment of the raft component caveolin-1 was induced at the adhesive contact between the cell surface and TAG-1 beads, indicating that enlarged rafts were generated. Photobleaching experiments showed that the lateral mobility of NrCAM increased with raft dispersion in these contact areas, further suggesting that TAG-1-coated beads induced the coalescence of lipid rafts. In conclusion, we propose that anchoring of NrCAM with the retrograde actin flow can be triggered by adhesive contacts via cooperative processes including interactions with the cytoplasmic tail, formation of cis-complex via the FNIII repeats, and lipid raft aggregation.

Indexed as

ActinsAnimalsBiological TransportCell Adhesion MoleculesCell Adhesion Molecules, NeuronalCell Line, TumorContactin 2CytoskeletonMembrane MicrodomainsProtein BindingProtein Structure, TertiaryRatsRecombinant Fusion ProteinsActinsCell Adhesion MoleculesCell Adhesion Molecules, NeuronalCntn2 protein, ratContactin 2NrCAM protein, ratRecombinant Fusion Proteins

Identifiers

PMID15254265
PMCPMC519160

What OpenQuestion holds

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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.