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

Feng, Kang LU ; Zhou, Xiao-Hong; Oohashi, Toshitaka; Mörgelin, Matthias LU ; Lustig, Ariel; Hirakawa, Satoshi; Ninomiya, Yoshifumi; Engel, Jürgen; Rauch, Uwe LU and Fässler, Reinhard (2002) In Journal of Biological Chemistry 277(29). p.26128-26135
Abstract
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... (More)
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. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Biological Chemistry
volume
277
issue
29
pages
26128 - 26135
publisher
ASBMB
external identifiers
  • wos:000176908700040
  • scopus:0037135575
ISSN
1083-351X
DOI
10.1074/jbc.M203722200
language
English
LU publication?
yes
id
1d1f9349-43ef-4501-b018-efd75862cf70 (old id 109336)
alternative location
http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=Retrieve&db=PubMed&list_uids=12000766&dopt=Abstract
date added to LUP
2007-07-19 14:54:25
date last changed
2017-05-28 03:50:25
@article{1d1f9349-43ef-4501-b018-efd75862cf70,
  abstract     = {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.},
  author       = {Feng, Kang and Zhou, Xiao-Hong and Oohashi, Toshitaka and Mörgelin, Matthias and Lustig, Ariel and Hirakawa, Satoshi and Ninomiya, Yoshifumi and Engel, Jürgen and Rauch, Uwe and Fässler, Reinhard},
  issn         = {1083-351X},
  language     = {eng},
  number       = {29},
  pages        = {26128--26135},
  publisher    = {ASBMB},
  series       = {Journal of Biological Chemistry},
  title        = {All four members of the Ten-m/Odz family of transmembrane proteins form dimers.},
  url          = {http://dx.doi.org/10.1074/jbc.M203722200},
  volume       = {277},
  year         = {2002},
}