Evidence map›Paper›PMID 10427099›Full record

ArticleThe Journal of cell biology1999

Characterization of integrin-tetraspanin adhesion complexes: role of tetraspanins in integrin signaling.

F Berditchevski, E Odintsova

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 120 papers.

0numbers the graph read from it
0cells of the map it votes in
120citing papers in PubMed
7.0field-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

120 citing papers in PubMed, 279 citations in OpenAlex.

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  5. Effect of radiotherapy on the DNA cargo and cellular uptake mechanisms of extracellular vesicles.Strahlentherapie und Onkologie : Organ der Deutschen Rontgengesellschaft ... [et al] · 2023
    Review
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  8. Review
  9. Review
  10. Review
  11. Review
  12. Arabidopsis Tetraspanins Facilitate Virus InfectionFrontiers in plant science · 2022
    Article
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  19. CD82 and Gangliosides Tune CD81 Membrane Behavior.International journal of molecular sciences · 2021
    Article
  20. Article

60 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

2 authors at 1 institution in 1 country.

F BerditchevskiCRC Institute for Cancer Studies, The University of Birmingham, Edgbaston, Birmingham, United Kingdom B15 2TA. f.beritchevski@bham.ac.uk
E Odintsova
University of Birmingham · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tetraspanins (or proteins from the transmembrane 4 superfamily, TM4SF) form membrane complexes with integrin receptors and are implicated in integrin-mediated cell migration. Here we characterized cellular localization, structural composition, and signaling properties of alpha3beta1-TM4SF adhesion complexes. Double-immunofluorescence staining showed that various TM4SF proteins, including CD9, CD63, CD81, CD82, and CD151 are colocalized within dot-like structures that are particularly abundant at the cell periphery. Differential extraction in conjunction with chemical cross-linking indicated that the cell surface fraction of alpha3beta1-TM4SF protein complexes may not be directly linked to the cytoskeleton. However, in cells treated with cytochalasin B alpha3beta1-TM4SF protein complexes are relocated into intracellular vesicles suggesting that actin cytoskeleton plays an important role in the distribution of tetraspanins into adhesion structures. Talin and MARCKS are partially codistributed with TM4SF proteins, whereas vinculin is not detected within the tetraspanin-containing adhesion structures. Attachment of serum-starved cells to the immobilized anti-TM4SF mAbs induced dephosphorylation of focal adhesion kinase (FAK). On the other hand, clustering of tetraspanins in cells attached to collagen enhanced tyrosine phosphorylation of FAK. Furthermore, ectopic expression of CD9 in fibrosarcoma cells affected adhesion-induced tyrosine phosphorylation of FAK, that correlated with the reorganization of the cortical actin cytoskeleton. These results show that tetraspanins can modulate integrin signaling, and point to a mechanism by which TM4SF proteins regulate cell motility.

Indexed as

Intracellular Signaling Peptides and ProteinsMembrane GlycoproteinsSignal TransductionActinsAntigens, CDBreast NeoplasmsCell AdhesionCell Adhesion MoleculesCulture Media, Serum-FreeCytochalasin BCytoskeletonExtracellular Matrix ProteinsFibrosarcomaFocal Adhesion Kinase 1Focal Adhesion Protein-Tyrosine KinasesHumansActinsAntigens, CDCD9 protein, humanCell Adhesion MoleculesCulture Media, Serum-FreeCytochalasin BExtracellular Matrix ProteinsFocal Adhesion Kinase 1Focal Adhesion Protein-Tyrosine KinasesIntegrin alpha3beta1IntegrinsIntracellular Signaling Peptides and ProteinsMARCKS protein, humanMembrane GlycoproteinsMembrane ProteinsMyristoylated Alanine-Rich C Kinase SubstrateNocodazoleProteinsProtein-Tyrosine KinasesPTK2 protein, humanTalinTetraspanin 29Vinculin

Identifiers

PMID10427099
PMCPMC2156181
OpenAlexW2047436557

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.