ArticleProceedings of the National Academy of Sciences of the United States of America2015
Diverse oligomeric states of CEACAM IgV domains.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
What it found
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Who cites it
43 citing papers in PubMed, 51 citations in OpenAlex.
- Dual-recognizing antibodies targeting CEACAMs in the tumor microenvironment: towards more precise targeting.Cell communication and signaling : CCS · 2026Review
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- Integrative Omics Analysis Reveals the Potential Value of CEACAM6 in Pan-Gastrointestinal Cancers.Immunity, inflammation and disease · 2026Article
- 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
- CEACAM6 facilitates gastric cancer progression through upregulating SLC27A2.Cancer gene therapy · 2025Article
- The influence of hypoxia-mediated CEACAM6 upregulation on epithelial cell and macrophage response in the context of gastric cancer.European journal of clinical investigation · 2024Article
- Structural aspects of CEACAM1 interactions.European journal of clinical investigation · 2024Review
- The role of CEACAMs in neutrophil function.European journal of clinical investigation · 2024Review
- Evolution of CEACAM pathogen decoy receptors in primates.European journal of clinical investigation · 2024Article
- Structural insights into epitope-paratope interactions of a monoclonal antibody targeting CEACAM5-expressing tumors.Nature communications · 2024Article
- Article
- Host-derived CEACAM-laden vesicles engage enterotoxigenicProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Host-derived CEACAM-laden vesicles engage enterotoxigenicbioRxiv : the preprint server for biology · 2024Article
- CEACAM6 expression and function in tumor biology: a comprehensive review.Discover oncology · 2024Review
- The emerging roles of CEACAM6 in human cancer (Review).International journal of oncology · 2024Review
- Editorial: Role of carcinoembryonic antigen-related cell adhesion molecules in pathogen responses, tumorigenicity, and immune modulation.Frontiers in immunology · 2024Article
- CT109-SN-38, a Novel Antibody-drug Conjugate with Dual Specificity for CEACAM5 and 6, Elicits Potent Killing of Pancreatic Cancer Cells.Current cancer drug targets · 2024Article
- Interactions of pathogenicFrontiers in immunology · 2023Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Carcinoembryonic antigen-related cell adhesion molecules (CEACAMs) comprise a large family of cell surface adhesion molecules that bind to themselves and other family members to carry out numerous cellular functions, including proliferation, signaling, differentiation, tumor suppression, and survival. They also play diverse and significant roles in immunity and infection. The formation of CEACAM oligomers is caused predominantly by interactions between their N-terminal IgV domains. Although X-ray crystal structures of CEACAM IgV domain homodimers have been described, how CEACAMs form heterodimers or remain monomers is poorly understood. To address this key aspect of CEACAM function, we determined the crystal structures of IgV domains that form a homodimeric CEACAM6 complex, monomeric CEACAM8, and a heterodimeric CEACAM6-CEACAM8 complex. To confirm and quantify these interactions in solution, we used analytical ultracentrifugation to measure the dimerization constants of CEACAM homodimers and isothermal titration calorimetry to determine the thermodynamic parameters and binding affinities of CEACAM heterodimers. We found the CEACAM6-CEACAM8 heterodimeric state to be substantially favored energetically relative to the CEACAM6 homodimer. Our data provide a molecular basis for the adoption of the diverse oligomeric states known to exist for CEACAMs and suggest ways in which CEACAM6 and CEACAM8 regulate the biological functions of one another, as well as of additional CEACAMs with which they interact, both in cis and in trans.
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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.