Mechanism and function of CEACAM1 splice isoforms

Eur J Clin Invest. 2024 Dec;54 Suppl 2(Suppl 2):e14350. doi: 10.1111/eci.14350.

Abstract

Background: Alternative splicing is a fundamental mechanism in the post-transcriptional regulation of genes. The multifunctional transmembrane glycoprotein receptor carcinoembryonic antigen-related cell adhesion molecule 1 (CEACAM1) undergoes extensive alternative splicing to allow for tunable functions in cell signalling, adhesion and modulation of immune and metabolic responses. Splice isoforms that differ in their ectodomain and short or long cytoplasmic tail (CEACAM1-S/CEACAM1-L) have distinct functional roles. The mechanisms that regulate CEACAM1 RNA splicing remain elusive.

Methods: This narrative review summarizes the current knowledge of the mechanism and function of CEACAM1 splice isoforms. Historical perspectives address the biological significance of the glycosylated Ig domains, the variable exon 7, and phosphorylation events that dictate its signal transduction pathways. The use of small antisense molecules to target mis-spliced variable exon 7 is discussed.

Results: The Ig variable-like N domain mediates cell adhesion and immune checkpoint inhibitory functions. Gly and Tyr residues in the transmembrane (TM) domain are essential for dimerization. Calmodulin, Calcium/Calmodulin-dependent protein kinase II delta (CamK2D), Actin and Annexin A2 are binding partners of CEACAM1-S. Homology studies of the muCEACAM1-S and huCEACAM1-S TM predict differences in their signal transduction pathways. Hypoxia-inducible factor 1-α (HIF-1-α) induces alternative splicing to produce CEACAM1-S under limited oxygen conditions. Antisense small molecules directed to exon 7 may correct faulty expression of the short and long cytoplasmic tail splicing isoforms.

Conclusion: More pre-clinical and clinical studies are needed to elucidate the precise mechanisms by which CEACAM1 RNA splicing may be exploited to develop targeted interventions towards novel therapeutic strategies.

Keywords: CEACAM1; alternative splicing; exons; inflammation; ischemia‐reperfusion injury; phosphorodiamidate morpholinos.

Publication types

  • Review

MeSH terms

  • Alternative Splicing* / genetics
  • Antigens, CD* / genetics
  • Antigens, CD* / metabolism
  • Calcium-Calmodulin-Dependent Protein Kinase Type 2 / genetics
  • Calcium-Calmodulin-Dependent Protein Kinase Type 2 / metabolism
  • Calmodulin / genetics
  • Calmodulin / metabolism
  • Cell Adhesion / genetics
  • Cell Adhesion / physiology
  • Cell Adhesion Molecules* / genetics
  • Cell Adhesion Molecules* / metabolism
  • Exons* / genetics
  • Glycosylation
  • Humans
  • Immune Checkpoint Inhibitors / therapeutic use
  • Phosphorylation
  • Protein Domains
  • Protein Isoforms* / genetics
  • Signal Transduction

Substances

  • Cell Adhesion Molecules
  • CD66 antigens
  • Antigens, CD
  • Protein Isoforms
  • Calcium-Calmodulin-Dependent Protein Kinase Type 2
  • Calmodulin
  • Immune Checkpoint Inhibitors