期刊
JOURNAL OF CELL BIOLOGY
卷 187, 期 4, 页码 553-567出版社
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.200904149
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资金
- 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
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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