| First Author | Feng K | Year | 2002 |
| Journal | J Biol Chem | Volume | 277 |
| Issue | 29 | Pages | 26128-35 |
| PubMed ID | 12000766 | Mgi Jnum | J:190001 |
| Mgi Id | MGI:5447626 | Doi | 10.1074/jbc.M203722200 |
| Citation | Feng K, et al. (2002) All four members of the Ten-m/Odz family of transmembrane proteins form dimers. J Biol Chem 277(29):26128-35 |
| abstractText | Ten-m/Odz/teneurins are a new family of four distinct type II transmembrane molecules. Their extracellular domains are composed of an array of eight consecutive EGF modules followed by a large globular domain. Two of the eight modules contain only 5 instead of the typical 6 cysteine residues and have the capability to dimerize in a covalent, disulfide-linked fashion. The structural properties of the extracellular domains of all four mouse Ten-m proteins have been analyzed using secreted, recombinant molecules produced by mammalian HEK-293 cells. Electron microscopic analysis supported by analytical ultracentrifugation data revealed that the recombinant extracellular domains of all Ten-m proteins formed homodimers. SDS-PAGE analysis under nonreducing conditions as well as negative staining after partial denaturation of the molecules indicated that the globular COOH-terminal domains of Ten-m1 and -m4 contained subdomains with a pronounced stability against denaturing agents, especially when compared with the homologous domains of Ten-m2 and -m3. Cotransfection experiments of mammalian cells with two different extracellular domains revealed that Ten-m molecules have also the ability to form heterodimers, a property that, combined with alternative splicing events, allows the formation of a multitude of molecules with different characteristics from a limited set of genes. |
