Evidence map›Paper›PMID 11179419›Full record

ArticleMolecular biology of the cell2001

Characterization of syntenin, a syndecan-binding PDZ protein, as a component of cell adhesion sites and microfilaments.

P Zimmermann, D Tomatis, M Rosas, J Grootjans, I Leenaerts, G Degeest, G Reekmans, C Coomans, G David

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.

0numbers the graph read from it
0cells of the map it votes in
84citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

84 citing papers in PubMed, 180 citations in OpenAlex.

  1. Article
  2. Dengue virus harnesses mosquito Syntenin to load and secrete viral RNA into salivary exosomes.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Article
  4. Exosomes are specialized vehicles to induce fibronectin assembly.bioRxiv : the preprint server for biology · 2025
    Article
  5. Article
  6. Article
  7. Exosomes: Methods for Isolation and Characterization in Biological Samples.Methods in molecular biology (Clifton, N.J.) · 2024
    Review
  8. PDZ scaffolds regulate extracellular vesicle production, composition, and uptake.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
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  10. Review
  11. Review
  12. Review
  13. Article
  14. Review
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  20. Article

24 more citing papers are in PubMed but not listed here.

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

9 authors at 1 institution in 1 country.

P ZimmermannLaboratory for Glycobiology and Developmental Genetics, Center for Human Genetics, University of Leuven, Leuven, B-3000 Belgium.
D Tomatis
M Rosas
J Grootjans
I Leenaerts
G Degeest
G Reekmans
C Coomans
G David
Vlaams Instituut voor Biotechnologie · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Syntenin is a PDZ protein that binds the cytoplasmic C-terminal FYA motif of the syndecans. Syntenin is widely expressed. In cell fractionation experiments, syntenin partitions between the cytosol and microsomes. Immunofluorescence microscopy localizes endogenous and epitope-tagged syntenin to cell adhesion sites, microfilaments, and the nucleus. Syntenin is composed of at least three domains. Both PDZ domains of syntenin are necessary to target reporter tags to the plasma membrane. The addition of a segment of 10 amino acids from the N-terminal domain of syntenin to these PDZ domains increases the localization of the tags to stress fibers and induces the formation of long, branching plasma membrane extensions. The addition of the complete N-terminal region, in contrast, reduces the localization of the tags to plasma membrane/adhesion sites and stress fibers, and reduces the morphotypical effects. Recombinant domains of syntenin with the highest plasma membrane localization display the lowest nuclear localization. Syndecan-1, E-cadherin, beta-catenin, and alpha-catenin colocalize with syntenin at cell-cell contacts in epithelial cells, and coimmunoprecipitate with syntenin from extracts of these cells. These results suggest a role for syntenin in the composition of adherens junctions and the regulation of plasma membrane dynamics, and imply a potential role for syntenin in nuclear processes.

Indexed as

Intracellular Signaling Peptides and ProteinsMembrane ProteinsActin CytoskeletonAmino Acid SequenceAnimalsCadherinsCarrier ProteinsCell AdhesionCell CommunicationCell MembraneCell NucleusCells, CulturedConserved SequenceCytosolEpithelial CellsHumansCadherinsCarrier ProteinsIntracellular Signaling Peptides and ProteinsMembrane GlycoproteinsMembrane ProteinsProteoglycansSDC1 protein, humanSdc1 protein, mouseSDCBP protein, humanSyndecan-1SyndecansSyntenins

Identifiers

PMID11179419
PMCPMC30947
OpenAlexW2144588996

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.