All four members of the Ten-m/Odz family of transmembrane proteins form dimers.
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/109336
- author
- 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
- organization
- publishing date
- 2002
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Biological Chemistry
- volume
- 277
- issue
- 29
- pages
- 26128 - 26135
- publisher
- American Society for Biochemistry and Molecular Biology
- external identifiers
-
- wos:000176908700040
- scopus:0037135575
- pmid:12000766
- ISSN
- 1083-351X
- DOI
- 10.1074/jbc.M203722200
- language
- English
- LU publication?
- yes
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Pathology, (Lund) (013030000), Department of Clinical Sciences, Lund (013230000), Vessel Wall Biology (013212028)
- 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
- 2016-04-01 12:38:05
- date last changed
- 2022-02-19 01:10:59
@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 = {{American Society for Biochemistry and Molecular Biology}},
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}},
doi = {{10.1074/jbc.M203722200}},
volume = {{277}},
year = {{2002}},
}