Journal
JOURNAL OF CELL BIOLOGY
Volume 187, Issue 4, Pages 553-567Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.200904149
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Funding
- Swedish Research Council [05200, 621-2005-5540]
- Swedish Cancer Foundation [07 0629]
- Marianne and Markus Wallenbergs Stiftelse
- Knut and Alice Wallenbergs Stiftelse
- Agouron Institute
- Swedish Foundation for Strategic Research
- Foundation for Knowledge and Competence Development
- European Union 3D-EM Network of Excellence
- Magnus Bergwalls Stiftelse
- Karolinska Institutet
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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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