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

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

Research output: Contribution to journalArticle

56 Citations (Scopus)

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. Co-transfection 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.

Original languageEnglish
Pages (from-to)26128-26135
Number of pages8
JournalJournal of Biological Chemistry
Volume277
Issue number29
DOIs
Publication statusPublished - Jul 19 2002

Fingerprint

Dimers
Negative Staining
Molecules
HEK293 Cells
Ultracentrifugation
Alternative Splicing
Epidermal Growth Factor
Disulfides
Transfection
Cysteine
Polyacrylamide Gel Electrophoresis
Proteins
Electrons
Denaturation
Genes
Structural properties
Cells
Experiments

ASJC Scopus subject areas

  • Biochemistry

Cite this

Feng, K., Zhou, X. H., Oohashi, T., Mörgelin, M., Lustig, A., Hirakawa, S., ... Fässler, R. (2002). All four members of the Ten-m/Odz family of transmembrane proteins form dimers. Journal of Biological Chemistry, 277(29), 26128-26135. https://doi.org/10.1074/jbc.M203722200

All four members of the Ten-m/Odz family of transmembrane proteins form dimers. / Feng, Kang; Zhou, Xiao Hong; Oohashi, Toshitaka; Mörgelin, Matthias; Lustig, Ariel; Hirakawa, Satoshi; Ninomiya, Yoshifumi; Engel, Jürgen; Rauch, Uwe; Fässler, Reinhard.

In: Journal of Biological Chemistry, Vol. 277, No. 29, 19.07.2002, p. 26128-26135.

Research output: Contribution to journalArticle

Feng, K, Zhou, XH, Oohashi, T, Mörgelin, M, Lustig, A, Hirakawa, S, Ninomiya, Y, Engel, J, Rauch, U & Fässler, R 2002, 'All four members of the Ten-m/Odz family of transmembrane proteins form dimers', Journal of Biological Chemistry, vol. 277, no. 29, pp. 26128-26135. https://doi.org/10.1074/jbc.M203722200
Feng, Kang ; Zhou, Xiao Hong ; Oohashi, Toshitaka ; Mörgelin, Matthias ; Lustig, Ariel ; Hirakawa, Satoshi ; Ninomiya, Yoshifumi ; Engel, Jürgen ; Rauch, Uwe ; Fässler, Reinhard. / All four members of the Ten-m/Odz family of transmembrane proteins form dimers. In: Journal of Biological Chemistry. 2002 ; Vol. 277, No. 29. pp. 26128-26135.
@article{fb3f62d14cce46cdb8c4ecaaeda5d7dc,
title = "All four members of the Ten-m/Odz family of transmembrane proteins form dimers",
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. Co-transfection 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 = "Kang Feng and Zhou, {Xiao Hong} and Toshitaka Oohashi and Matthias M{\"o}rgelin and Ariel Lustig and Satoshi Hirakawa and Yoshifumi Ninomiya and J{\"u}rgen Engel and Uwe Rauch and Reinhard F{\"a}ssler",
year = "2002",
month = "7",
day = "19",
doi = "10.1074/jbc.M203722200",
language = "English",
volume = "277",
pages = "26128--26135",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "29",

}

TY - JOUR

T1 - All four members of the Ten-m/Odz family of transmembrane proteins form dimers

AU - Feng, Kang

AU - Zhou, Xiao Hong

AU - Oohashi, Toshitaka

AU - Mörgelin, Matthias

AU - Lustig, Ariel

AU - Hirakawa, Satoshi

AU - Ninomiya, Yoshifumi

AU - Engel, Jürgen

AU - Rauch, Uwe

AU - Fässler, Reinhard

PY - 2002/7/19

Y1 - 2002/7/19

N2 - 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. Co-transfection 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.

AB - 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. Co-transfection 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.

UR - http://www.scopus.com/inward/record.url?scp=0037135575&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0037135575&partnerID=8YFLogxK

U2 - 10.1074/jbc.M203722200

DO - 10.1074/jbc.M203722200

M3 - Article

C2 - 12000766

AN - SCOPUS:0037135575

VL - 277

SP - 26128

EP - 26135

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 29

ER -