All four members of the Ten-m/Odz family of transmembrane proteins form dimers.
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.
Feng
Kang
K
Department of Experimental Pathology, Lund University, S-221 85 Lund, Sweden.
Zhou
Xiao-Hong
XH
Oohashi
Toshitaka
T
Mörgelin
Matthias
M
Lustig
Ariel
A
Hirakawa
Satoshi
S
Ninomiya
Yoshifumi
Y
Engel
Jürgen
J
Rauch
Uwe
U
Fässler
Reinhard
R
D000595:Amino Acid Sequence; D000818:Animals; D030161:Avian Proteins; D019281:Dimerization; D004591:Electrophoresis, Polyacrylamide Gel; D008565:Membrane Proteins / Q000737:chemistry; D051379:Mice; D008854:Microscopy, Electron; D008958:Models, Molecular; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009419:Nerve Tissue Proteins / Q000737:chemistry; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry; D019063:Tenascin / Q000737:chemistry*; D029961:Zebrafish Proteins
D030161:Avian Proteins; D008565:Membrane Proteins; D009419:Nerve Tissue Proteins; D011994:Recombinant Proteins; C583794:Ten-m2 protein, mouse; D019063:Tenascin; D029961:Zebrafish Proteins; C120530:teneurin-1; C402591:teneurin-2 protein, chicken; C405067:tenm3 protein, zebrafish; C405068:tenm4 protein, zebrafish