Evidence map›Paper›PMID 8636238›Full record

ArticleThe Journal of cell biology1996

Neuroglian-mediated cell adhesion induces assembly of the membrane skeleton at cell contact sites.

R R Dubreuil, G MacVicar, S Dissanayake, C Liu, D Homer, M Hortsch

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
8.9field-weighted citation impact, top 2% 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

46 citing papers in PubMed, 126 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Axonal ensheathment and septate junction formation in the peripheral nervous system of Drosophila.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2006
    Article
  20. Review
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 1 institution in 1 country.

R R DubreuilDepartment of Pharmacological & Physiological Sciences, University of Chicago, Illinois 60637, USA.
G MacVicar
S Dissanayake
C Liu
D Homer
M Hortsch
Department of Physiological Sciences · RU

Funding

GENETIC STUDIES OF THE MEMBRANE SKELETONR01GM049301 · NIGMS · UNIVERSITY OF ILLINOIS AT CHICAGO · PI DUBREUIL, RONALD R · 1995 to 2004
$1.1M
L1-MEDIATED RECRUITMENT OF THE MEMBRANE SKELETONR01HD029388 · NICHD · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI HORTSCH, MICHAEL · 1998 to 2002
$681k
DROSOPHILA NEUROGLIAN IN CELLULAR REGULATIONR29HD029388 · NICHD · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI HORTSCH, MICHAEL · 1993 to 1997
–
NICHD NIH HHS HD29388NIGMS NIH HHS GM49301
6 · The paper itself

Abstract

The protein ankyrin links integral membrane proteins to the spectrin-based membrane skeleton. Ankyrin is often concentrated within restricted membrane domains of polarized epithelia and neurons, but the mechanisms responsible for membrane targeting and its segregation within a continuous lipid bilayer remain unexplained. We provide evidence that neuroglian, a cell adhesion molecule related to L1 and neurofascin, can transmit positional information directly to ankyrin and thereby polarize its distribution in Drosophila S2 tissue culture cells. Ankyrin was not normally associated with the plasma membrane of these cells. Upon expression of an inducible neuroglian minigene, however, cells aggregated into large clusters and ankyrin became concentrated at sites of cell-cell contact. Spectrin was also recruited to sites of cell contact in response to neuroglian expression. The accumulation of ankyrin at cell contacts required the presence of the cytoplasmic domain of neuroglian since a glycosyl phosphatidylinositol-linked form of neuroglian failed to recruit ankyrin to sites of cell-cell contact. Double-labeling experiments revealed that, whereas ankyrin was strictly associated with sites of cell-cell contact, neuroglian was more broadly distributed over the cell surface. A direct interaction between neuroglian and ankyrin was demonstrated using yeast two-hybrid analysis. Thus, neuroglian appears to be activated by extracellular adhesion so that ankyrin and the membrane skeleton selectively associate with sites of cell contact and not with other regions of the plasma membrane.

Indexed as

AnimalsAnkyrinsBase SequenceCell AdhesionCell Adhesion Molecules, NeuronalCells, CulturedCytoskeletonDrosophilaDrosophila ProteinsFluorescent Antibody TechniqueIntercellular JunctionsMembrane ProteinsMolecular Sequence DataRecombinant ProteinsSpectrinYeastsAnkyrinsCell Adhesion Molecules, NeuronalDrosophila ProteinsMembrane ProteinsNrg protein, DrosophilaRecombinant ProteinsSpectrin

Identifiers

PMID8636238
PMCPMC2120821
OpenAlexW2151665992

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.