Evidence map›Paper›PMID 11470827›Full record

ArticleThe Journal of cell biology2001

MUP-4 is a novel transmembrane protein with functions in epithelial cell adhesion in Caenorhabditis elegans.

L Hong, T Elbl, J Ward, C Franzini-Armstrong, K K Rybicka, B K Gatewood, D L Baillie, E A Bucher

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
1.1field-weighted citation impact, top 27% 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

31 citing papers in PubMed, 67 citations in OpenAlex.

  1. Article
  2. Apical spectrin organizes cortical actin filament bundles to patternbioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Cells · 2023
    Article
  9. Large-scale proteomic analysis ofFrontiers in parasitology · 2023
    Article
  10. Article
  11. Article
  12. Article
  13. Journal of developmental biology · 2020
    Review
  14. Article
  15. Game of Tissues: How the Epidermis ThronesJournal of developmental biology · 2020
    Review
  16. Article
  17. Article
  18. Molting inWorm · 2017
    Review
  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

8 authors at 2 institutions in 2 countries.

L HongDepartment of Cell and Developmental Biology, University of Pennsylvania, School of Medicine, Philadelphia, PA 19104, USA.
T Elbl
J Ward
C Franzini-Armstrong
K K Rybicka
B K Gatewood
D L Baillie
E A Bucher
University of Pennsylvania · USSimon Fraser University · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tissue functions and mechanical coupling of cells must be integrated throughout development. A striking example of this coupling is the interactions of body wall muscle and hypodermal cells in Caenorhabditis elegans. These tissues are intimately associated in development and their interactions generate structures that provide a continuous mechanical link to transmit muscle forces across the hypodermis to the cuticle. Previously, we established that mup-4 is essential in embryonic epithelial (hypodermal) morphogenesis and maintenance of muscle position. Here, we report that mup-4 encodes a novel transmembrane protein that is required for attachments between the apical epithelial surface and the cuticular matrix. Its extracellular domain includes epidermal growth factor-like repeats, a von Willebrand factor A domain, and two sea urchin enterokinase modules. Its intracellular domain is homologous to filaggrin, an intermediate filament (IF)-associated protein that regulates IF compaction and that has not previously been reported as part of a junctional complex. MUP-4 colocalizes with epithelial hemidesmosomes overlying body wall muscles, beginning at the time of embryonic cuticle maturation, as well as with other sites of mechanical coupling. These findings support that MUP-4 is a junctional protein that functions in IF tethering, cell-matrix adherence, and mechanical coupling of tissues.

Indexed as

Caenorhabditis elegans ProteinsAnimalsAnimals, Genetically ModifiedCaenorhabditis elegansCell AdhesionCell Adhesion MoleculesCloning, MolecularEmbryo, NonmammalianEpithelial CellsGene ExpressionGreen Fluorescent ProteinsHelminth ProteinsHemidesmosomesLarvaLuminescent ProteinsMembrane ProteinsCaenorhabditis elegans ProteinsCell Adhesion MoleculesGreen Fluorescent ProteinsHelminth ProteinsLuminescent ProteinsMembrane ProteinsMUP-4 protein, C elegansRNA, Double-Stranded

Identifiers

PMID11470827
PMCPMC2150763
OpenAlexW1981554736

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.