Evidence map›Paper›PMID 19948503›Full record

ArticleThe Journal of cell biology2009

Homophilic adhesion and CEACAM1-S regulate dimerization of CEACAM1-L and recruitment of SHP-2 and c-Src.

Mario M Müller, Esther Klaile, Olga Vorontsova, Bernhard B Singer, Björn Obrink

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The Journal of cell biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

45 citing papers in PubMed, 70 citations in OpenAlex.

  1. Article
  2. Neutrophil CEACAMs and the Inflammatory Response toJournal of innate immunity · 2026
    Review
  3. Article
  4. Structural aspects of CEACAM1 interactions.European journal of clinical investigation · 2024
    Review
  5. The role of CEACAMs in neutrophil function.European journal of clinical investigation · 2024
    Review
  6. CEACAM1 in vascular homeostasis and inflammation.European journal of clinical investigation · 2024
    Review
  7. Review
  8. Review
  9. Effects ofFrontiers in immunology · 2023
    Review
  10. Review
  11. Article
  12. Article
  13. Review
  14. Cysteine Residues inMicroorganisms · 2020
    Article
  15. Pathogenic interactions betweenIranian journal of basic medical sciences · 2019
    Review
  16. Review
  17. Review
  18. Article
  19. The EMBO journal · 2018
    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

5 authors at 2 institutions in 2 countries.

Mario M MüllerDepartment of Cell and Molecular Biology, Karolinska Institutet, 171 77 Stockholm, Sweden.
Esther Klaile
Olga Vorontsova
Bernhard B Singer
Björn Obrink
Karolinska Institutet · SEEssen University Hospital · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Carcinoembryonic antigen (CEA)-related cell adhesion molecule 1 (CAM1 [CEACAM1]) mediates homophilic cell adhesion and regulates signaling. Although there is evidence that CEACAM1 binds and activates SHP-1, SHP-2, and c-Src, knowledge about the mechanism of transmembrane signaling is lacking. To analyze the regulation of SHP-1/SHP-2/c-Src binding, we expressed various CFP/YFP-tagged CEACAM1 isoforms in epithelial cells. The supramolecular organization of CEACAM1 was examined by cross-linking, coclustering, coimmunoprecipitation, and fluorescence resonance energy transfer. SHP-1/SHP-2/c-Src binding was monitored by coimmunoprecipitation and phosphotyrosine-induced recruitment to CEACAM1-L in cellular monolayers. We find that trans-homophilic CEACAM1 binding induces cis-dimerization by an allosteric mechanism transmitted by the N-terminal immunoglobulin-like domain. The balance of SHP-2 and c-Src binding is dependent on the monomer/dimer equilibrium of CEACAM1-L and is regulated by trans-binding, whereas SHP-1 does not bind under physiological conditions. CEACAM1-L homodimer formation is reduced by coexpression of CEACAM1-S and modulated by antibody ligation. These data suggest that transmembrane signaling by CEACAM1 operates by alteration of the monomer/dimer equilibrium, which leads to changes in the SHP-2/c-Src-binding ratio.

Indexed as

AnimalsAntigens, CDCell AdhesionCell Adhesion MoleculesCell Line, TumorCell MembraneDimerizationGene SilencingPeptide FragmentsProtein BindingProtein IsoformsProtein TransportProtein Tyrosine Phosphatase, Non-Receptor Type 11RatsSignal Transductionsrc-Family KinasesAntigens, CDCD66 antigensCell Adhesion MoleculesPeptide FragmentsProtein IsoformsProtein Tyrosine Phosphatase, Non-Receptor Type 11src-Family Kinases

Identifiers

PMID19948503
PMCPMC2779222
OpenAlexW2039525305

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.