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Review
. 2014 Apr 15:12:27.
doi: 10.1186/1478-811X-12-27.

Signaling by epithelial members of the CEACAM family - mucosal docking sites for pathogenic bacteria

Arnaud Kengmo Tchoupa, Tamara Schuhmacher, Christof R Hauck  1
Affiliations
Review

Signaling by epithelial members of the CEACAM family - mucosal docking sites for pathogenic bacteria

Arnaud Kengmo Tchoupa et al. Cell Commun Signal. .

Abstract

Carcinoembryonic antigen-related cell adhesion molecules (CEACAMs) comprise a group of immunoglobulin-related vertebrate glycoproteins. Several family members, including CEACAM1, CEA, and CEACAM6, are found on epithelial tissues throughout the human body. As they modulate diverse cellular functions, their signaling capacity is in the focus of current research. In this review we will summarize the knowledge about common signaling processes initiated by epithelial CEACAMs and suggest a model of signal transduction by CEACAM family members lacking significant cytoplasmic domains. As pathogenic and non-pathogenic bacteria exploit these receptors during mucosal colonization, we try to highlight the connection between CEACAMs, microbes, and cellular responses. Special emphasis in this context is placed on the functional interplay between CEACAMs and integrins that influences matrix adhesion of epithelial cells. The cooperation between these two receptor families provides an intriguing example of the fine tuning of cellular responses and their manipulation by specialized microorganisms.

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Figures

Figure 1
Figure 1
The human CEACAM family. Schematic depiction of the twelve members of the human carcinoembryonic antigen-related cell adhesion molecules. The red spheres indicate IgV-like domains, the blue spheres indicate IgC2-like domains, which are stabilized by disulfide bonds (S-S). The green spirals indicate transmembrane helices. GPI-anchors are depicted in the form of a green arrow ending in the lipid bilayer. CEACAM20 encodes only a partial IgV-like domain (N*). Graph modified from http://www.carcinoembryonic-antigen.de/.
Figure 2
Figure 2
Signaling initiated by epithelial CEACAMs. Schematic summary of recent findings with regard to CEACAM-initiated signaling events in epithelial cells. Upon ligand binding, CEACAM1 forms oligomers supported by cis-interactions between the extracellular and the transmembrane domains (1) and is recruited to membrane microdomains (2). GPI-anchored epithelial CEACAMs, such as CEA or CEACAM6, constitutively localize to membrane microdomains (3). In membrane microdomains, epithelial CEACAMs connect to putative co-receptor(s) (black) via extracellular IgC2-like domains (4). Intracellular signaling triggered by epithelial CEACAMs either directly or indirectly via co-receptor(s) leads to phosphatidylinositol-3’-kinase dependent signaling processes connected to receptor-mediated endocytosis (5). Furthermore, stimulation of epithelial CEACAMs triggers novel gene expression events, e.g. de novo expression of CD105, which extracts zyxin from basal integrin-rich focal adhesion sites (6), resulting in increased integrin activity and enhanced binding to the basal extracellular matrix (ECM) (7).
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