Evidence map›Paper›PMID 24005674›Full record

ArticleThe Journal of biological chemistry2013

Inside-out signaling promotes dynamic changes in the carcinoembryonic antigen-related cellular adhesion molecule 1 (CEACAM1) oligomeric state to control its cell adhesion properties.

Prerna C Patel, Hannah S W Lee, Aaron Y K Ming, Arianna Rath, Charles M Deber, Christopher M Yip, Jonathan V Rocheleau, Scott D Gray-Owen

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.1field-weighted citation impact, top 14% 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

28 citing papers in PubMed, 54 citations in OpenAlex.

  1. C4BP occludes the non-opsonic interaction ofInfection and immunity · 2026
    Article
  2. Article
  3. Article
  4. C4BP occludes the non-opsonic interaction ofbioRxiv : the preprint server for biology · 2026
    Article
  5. Neutrophil CEACAMs and the Inflammatory Response toJournal of innate immunity · 2026
    Review
  6. Mechanism and function of CEACAM1 splice isoforms.European journal of clinical investigation · 2024
    Review
  7. Structural aspects of CEACAM1 interactions.European journal of clinical investigation · 2024
    Review
  8. CEACAM1 in vascular homeostasis and inflammation.European journal of clinical investigation · 2024
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. CEACAM1 promotes CD8Nature communications · 2018
    Article
  20. Neural immunoglobulin superfamily interaction networks.Current opinion in neurobiology · 2017
    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

8 authors at 3 institutions in 2 countries.

Prerna C PatelFrom the Department of Molecular Genetics and.
Hannah S W Lee
Aaron Y K Ming
Arianna Rath
Charles M Deber
Christopher M Yip
Jonathan V Rocheleau
Scott D Gray-Owen
Laboratory of Molecular Genetics · PLUniversity of Toronto · CAHospital for Sick Children · CA

Funding

Canadian Institutes of Health Research 365861-09Canadian Institutes of Health Research FRN-5810
6 · The paper itself

Abstract

Cell-cell contacts are fundamental to multicellular organisms and are subject to exquisite levels of control. The carcinoembryonic antigen-related cell adhesion molecule 1 (CEACAM1) can engage in both cis-homophilic (parallel) oligomerization and trans-homophilic (anti-parallel) binding. In this study, we establish that the CEACAM1 transmembrane domain has a propensity to form cis-dimers via the transmembrane-embedded (432)GXXXG(436) motif and that this basal state is overcome when activated calmodulin binds to the CEACAM1 cytoplasmic domain. Although mutation of the (432)GXXXG(436) motif reduced CEACAM1 oligomerization, it did not affect surface localization of the receptor or influence CEACAM1-dependent cellular invasion by the pathogenic Neisseria. The mutation did, however, have a striking effect on CEACAM1-dependent cellular aggregation, increasing both the kinetics of cell-cell association and the size of cellular aggregates formed. CEACAM1 association with tyrosine kinase c-Src and tyrosine phosphatases SHP-1 and SHP-2 was not affected by the (432)GXXXG(436) mutation, consistent with their association with the monomeric form of wild type CEACAM1. Collectively, our results establish that a dynamic oligomer-to-monomer shift in surface-expressed CEACAM1 facilitates trans-homophilic binding and downstream effector signaling.

Indexed as

Protein MultimerizationSignal TransductionAmino Acid MotifsAmino Acid SequenceAntigens, CDCalciumCalmodulinCell AdhesionCell Adhesion MoleculesCell MembraneHeLa CellsHumansImmunoblottingMicroscopy, ConfocalModels, MolecularMolecular Sequence DataAntigens, CDCalciumCalmodulinCD66 antigensCell Adhesion MoleculesProtein Tyrosine Phosphatase, Non-Receptor Type 11Protein Tyrosine Phosphatase, Non-Receptor Type 6src-Family KinasesBacterial AdhesionCalcium SignalingCalmodulinCancerCarcinoembryonic Antigen-related Cell Adhesion MoleculeCEACAM1Cell AdhesionHomodimerHomophilic BindingMembrane Proteins

Identifiers

PMID24005674
PMCPMC3795263
OpenAlexW2054049637

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.