Title |
The EGF-TM7 family: a postgenomic view
|
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Published in |
Immunogenetics, November 2003
|
DOI | 10.1007/s00251-003-0625-2 |
Pubmed ID | |
Authors |
Mark J. Kwakkenbos, Else N. Kop, Martin Stacey, Mourad Matmati, Siamon Gordon, Hsi-Hsien Lin, Jörg Hamann |
Abstract |
With the human and mouse genome projects now completed, the receptor repertoire of mammalian cells has finally been elucidated. The EGF-TM7 receptors are a family of class B seven-span transmembrane (TM7) receptors predominantly expressed by cells of the immune system. Within the large TM7 superfamily, the molecular structure and ligand-binding properties of EGF-TM7 receptors are unique. Derived from the processing of a single polypeptide, they are expressed at the cell surface as heterodimers consisting of a large extracellular region associated with a TM7 moiety. Through a variable number of N-terminal epidermal growth factor (EGF)-like domains, EGF-TM7 receptors interact with cellular ligands such as CD55 and chondroitin sulfate. Recent in vivo studies demonstrate a role of the EGF-TM7 receptor CD97 in leukocyte migration. The different number of EGF-TM7 genes in man compared with mice, the chimeric nature of EMR2 and the inactivation of human EMR4 point toward a still-evolving receptor family. Here we discuss the currently available information on this intriguing receptor family. |
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