ArticleThe Journal of cell biology2009
The CEACAM1 N-terminal Ig domain mediates cis- and trans-binding and is essential for allosteric rearrangements of CEACAM1 microclusters.
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 42 papers.
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Who cites it
42 citing papers in PubMed.
- C4BP occludes the non-opsonic interaction ofInfection and immunity · 2026Article
- C4BP occludes the non-opsonic interaction ofbioRxiv : the preprint server for biology · 2026Article
- Neutrophil CEACAMs and the Inflammatory Response toJournal of innate immunity · 2026Review
- Article
- Exploring the interactions of integrins and CEACAM6 (Review).Experimental and therapeutic medicine · 2025Review
- Binding ofProceedings of the National Academy of Sciences of the United States of America · 2025Article
- The role of CEACAMs in neutrophil function.European journal of clinical investigation · 2024Review
- Structural aspects of CEACAM1 interactions.European journal of clinical investigation · 2024Review
- Mechanism and function of CEACAM1 splice isoforms.European journal of clinical investigation · 2024Review
- CEACAM1 Is a Prognostic Biomarker and Correlated with Immune Cell Infiltration in Clear Cell Renal Cell Carcinoma.Disease markers · 2023Article
- Effects ofFrontiers in immunology · 2023Review
- Glycan Conformation in the Heavily Glycosylated Protein, CEACAM1.ACS chemical biology · 2022Article
- Structural analysis of human CEACAM1 oligomerization.Communications biology · 2022Article
- Human CEACAM1 N-domain dimerization is independent from glycan modifications.Structure (London, England : 1993) · 2022Article
- Structural basis of the dynamic human CEACAM1 monomer-dimer equilibrium.Communications biology · 2021Article
- Structural characterization of a dimeric complex between the short cytoplasmic domain of CEACAM1 and the pseudo tetramer of S100A10-Annexin A2 using NMR and molecular dynamics.Biochimica et biophysica acta. Biomembranes · 2021Article
- Neutrophil Extracellular Trap-Associated CEACAM1 as a Putative Therapeutic Target to Prevent Metastatic Progression of Colon Carcinoma.Journal of immunology (Baltimore, Md. : 1950) · 2020Article
- Structure of mouse coronavirus spike protein complexed with receptor reveals mechanism for viral entry.PLoS pathogens · 2020Article
- Pathogenic interactions betweenIranian journal of basic medical sciences · 2019Review
- CEACAM1 structure and function in immunity and its therapeutic implications.Seminars in immunology · 2019Review
Corrections and comments
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cell adhesion molecules (CAMs) sense the extracellular microenvironment and transmit signals to the intracellular compartment. In this investigation, we addressed the mechanism of signal generation by ectodomains of single-pass transmembrane homophilic CAMs. We analyzed the structure and homophilic interactions of carcinoembryonic antigen (CEA)-related CAM 1 (CEACAM1), which regulates cell proliferation, apoptosis, motility, morphogenesis, and microbial responses. Soluble and membrane-attached CEACAM1 ectodomains were investigated by surface plasmon resonance-based biosensor analysis, molecular electron tomography, and chemical cross-linking. The CEACAM1 ectodomain, which is composed of four glycosylated immunoglobulin-like (Ig) domains, is highly flexible and participates in both antiparallel (trans) and parallel (cis) homophilic binding. Membrane-attached CEACAM1 ectodomains form microclusters in which all four Ig domains participate. Trans-binding between the N-terminal Ig domains increases formation of CEACAM1 cis-dimers and changes CEACAM1 interactions within the microclusters. These data suggest that CEACAM1 transmembrane signaling is initiated by adhesion-regulated changes of cis-interactions that are transmitted to the inner phase of the plasma membrane.
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