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All four members of the Ten-m/Odz family of transmembrane proteins form dimers.

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Author

  • Kang Feng
  • Xiao-Hong Zhou
  • Toshitaka Oohashi
  • Matthias Mörgelin
  • Ariel Lustig
  • Satoshi Hirakawa
  • Yoshifumi Ninomiya
  • Jürgen Engel
  • Uwe Rauch
  • Reinhard Fässler

Summary, in English

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.

Publishing year

2002

Language

English

Pages

26128-26135

Publication/Series

Journal of Biological Chemistry

Volume

277

Issue

29

Document type

Journal article

Publisher

American Society for Biochemistry and Molecular Biology

Topic

  • Cancer and Oncology

Status

Published

Research group

  • Vessel Wall Biology

ISBN/ISSN/Other

  • ISSN: 1083-351X