ArticleThe Journal of biological chemistry2016
Glycosylation Alters Dimerization Properties of a Cell-surface Signaling Protein, Carcinoembryonic Antigen-related Cell Adhesion Molecule 1 (CEACAM1).
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 22 papers.
What it found
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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.
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.
Who cites it
22 citing papers in PubMed, 36 citations in OpenAlex.
- Inhibitory pattern recognition receptors: lessons from LAIR1.Nature reviews. Immunology · 2025Review
- Current investigation of carcinoembryonic antigen cell adhesion molecule (CEACAM) biology summary of the 32nd CEA symposium: 20-23 September 2024. Würzburg, Germany.European journal of clinical investigation · 2024Article
- Carcinoembryonic antigen-related cell adhesion molecule 1 in cancer: Blessing or curse?European journal of clinical investigation · 2024Review
- The role of carcinoembryonic antigen-related cell adhesion molecule 1 in cancer.Frontiers in immunology · 2023Review
- Glycan Conformation in the Heavily Glycosylated Protein, CEACAM1.ACS chemical biology · 2022Article
- AssignSLP_GUI, a software tool exploiting AI for NMR resonance assignment of sparsely labeled proteins.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2022Article
- Site-to-site cross-talk in OST-B glycosylation of hCEACAM1-IgV.Proceedings of the National Academy of Sciences of the United States of America · 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
- An investigation into the role of inherited CEACAM gene family variants and colorectal cancer risk.BMC research notes · 2022Article
- Article
- Sparse isotope labeling for nuclear magnetic resonance (NMR) of glycoproteins using 13C-glucose.Glycobiology · 2021Article
- 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
- Isoforms of RNF128 Regulate the Stability of Mutant P53 in Barrett's Esophageal Cells.Gastroenterology · 2020Article
- Evaluation of the Anti-Tumor Activity of the Humanized Monoclonal Antibody NEO-201 in Preclinical Models of Ovarian Cancer.Frontiers in oncology · 2020Article
- Pathogenic interactions betweenIranian journal of basic medical sciences · 2019Review
- CEACAM1 structure and function in immunity and its therapeutic implications.Seminars in immunology · 2019Review
- Molecular Cloning and Bioinformatics Analysis ofInternational journal of molecular sciences · 2019Article
- Structural Characterization of a Heparan Sulfate Pentamer Interacting with LAR-Ig1-2.Biochemistry · 2018Article
Corrections and comments
- Erratum issued
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Human carcinoembryonic antigen-related cell adhesion molecule 1 (C?/Au: EACAM1) is a cell-surface signaling molecule involved in cell adhesion, proliferation, and immune response. It is also implicated in cancer angiogenesis, progression, and metastasis. This diverse set of effects likely arises as a result of the numerous homophilic and heterophilic interactions that CEACAM1 can have with itself and other molecules. Its N-terminal Ig variable (IgV) domain has been suggested to be a principal player in these interactions. Previous crystal structures of the β-sandwich-like IgV domain have been produced using Escherichia coli-expressed material, which lacks native glycosylation. These have led to distinctly different proposals for dimer interfaces, one involving interactions of ABED β-strands and the other involving GFCC'C″ β-strands, with the former burying one prominent glycosylation site. These structures raise questions as to which form may exist in solution and what the effect of glycosylation may have on this form. Here, we use NMR cross-correlation measurements to examine the effect of glycosylation on CEACAM1-IgV dimerization and use residual dipolar coupling (RDC) measurements to characterize the solution structure of the non-glycosylated form. Our findings demonstrate that even addition of a single N-linked GlcNAc at potential glycosylation sites inhibits dimer formation. Surprisingly, RDC data collected on E. coli expressed material in solution indicate that a dimer using the non-glycosylated GFCC'C″ interface is preferred even in the absence of glycosylation. The results open new questions about what other factors may facilitate dimerization of CEACAM1 in vivo, and what roles glycosylation may play in heterophylic interactions.
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Registered trials
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.