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Mouse ten-m/Odz is a new family of dimeric type II transmembrane proteins expressed in many tissues

Oohashi, T; Zhou, Xiaohong LU ; Feng, Kang LU ; Richter, B; Mörgelin, Matthias LU ; Perez, Maria Thereza LU ; Su, W D; Chiquet-Ehrismann, R; Rauch, Uwe LU and Fässler, Reinhard LU (1999) In Journal of Cell Biology 145(3). p.563-577
Abstract
The Drosophila gene ten-m/odz is the only pair rule gene identified to date which is not a transcription factor. In an attempt to analyze the structure and the function of ten-m/odz in mouse, we isolated four murine ten-m cDNAs which code for proteins of 2,700-2, 800 amino acids. All four proteins (Ten-m1-4) lack signal peptides at the NH2 terminus, but contain a short hydrophobic domain characteristic of transmembrane proteins, 300-400 amino acids after the NH2 terminus. About 200 amino acids COOH-terminal to this hydrophobic region are eight consecutive EGF-like domains. Cell transfection, biochemical, and electronmicroscopic studies suggest that Ten-m1 is a dimeric type II transmembrane protein. Expression of fusion proteins composed of... (More)
The Drosophila gene ten-m/odz is the only pair rule gene identified to date which is not a transcription factor. In an attempt to analyze the structure and the function of ten-m/odz in mouse, we isolated four murine ten-m cDNAs which code for proteins of 2,700-2, 800 amino acids. All four proteins (Ten-m1-4) lack signal peptides at the NH2 terminus, but contain a short hydrophobic domain characteristic of transmembrane proteins, 300-400 amino acids after the NH2 terminus. About 200 amino acids COOH-terminal to this hydrophobic region are eight consecutive EGF-like domains. Cell transfection, biochemical, and electronmicroscopic studies suggest that Ten-m1 is a dimeric type II transmembrane protein. Expression of fusion proteins composed of the NH2-terminal and hydrophobic domain of ten-m1 attached to the alkaline phosphatase reporter gene resulted in membrane-associated staining of the alkaline phosphatase. Electronmicroscopic and electrophoretic analysis of a secreted form of the extracellular domain of Ten-m1 showed that Ten-m1 is a disulfide-linked dimer and that the dimerization is mediated by EGF-like modules 2 and 5 which contain an odd number of cysteines. Northern blot and immunohistochemical analyses revealed widespread expression of mouse ten-m genes, with most prominent expression in brain. All four ten-m genes can be expressed in variously spliced mRNA isoforms. The extracellular domain of Ten-m1 fused to an alkaline phosphatase reporter bound to specific regions in many tissues which were partially overlapping with the Ten-m1 immunostaining. Far Western assays and electronmicroscopy demonstrated that Ten-m1 can bind to itself. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
epidermal growth factor, pair rule, ten-m/odz, transmembrane protein
in
Journal of Cell Biology
volume
145
issue
3
pages
563 - 577
publisher
Rockefeller University Press
external identifiers
  • pmid:10225957
  • scopus:0033519207
ISSN
0021-9525
language
English
LU publication?
yes
id
b32dc2f3-926c-417f-8793-bbb058614038 (old id 1115468)
alternative location
http://www.jcb.org/cgi/content/full/145/3/563
date added to LUP
2008-07-08 09:52:46
date last changed
2017-01-01 04:20:42
@article{b32dc2f3-926c-417f-8793-bbb058614038,
  abstract     = {The Drosophila gene ten-m/odz is the only pair rule gene identified to date which is not a transcription factor. In an attempt to analyze the structure and the function of ten-m/odz in mouse, we isolated four murine ten-m cDNAs which code for proteins of 2,700-2, 800 amino acids. All four proteins (Ten-m1-4) lack signal peptides at the NH2 terminus, but contain a short hydrophobic domain characteristic of transmembrane proteins, 300-400 amino acids after the NH2 terminus. About 200 amino acids COOH-terminal to this hydrophobic region are eight consecutive EGF-like domains. Cell transfection, biochemical, and electronmicroscopic studies suggest that Ten-m1 is a dimeric type II transmembrane protein. Expression of fusion proteins composed of the NH2-terminal and hydrophobic domain of ten-m1 attached to the alkaline phosphatase reporter gene resulted in membrane-associated staining of the alkaline phosphatase. Electronmicroscopic and electrophoretic analysis of a secreted form of the extracellular domain of Ten-m1 showed that Ten-m1 is a disulfide-linked dimer and that the dimerization is mediated by EGF-like modules 2 and 5 which contain an odd number of cysteines. Northern blot and immunohistochemical analyses revealed widespread expression of mouse ten-m genes, with most prominent expression in brain. All four ten-m genes can be expressed in variously spliced mRNA isoforms. The extracellular domain of Ten-m1 fused to an alkaline phosphatase reporter bound to specific regions in many tissues which were partially overlapping with the Ten-m1 immunostaining. Far Western assays and electronmicroscopy demonstrated that Ten-m1 can bind to itself.},
  author       = {Oohashi, T and Zhou, Xiaohong and Feng, Kang and Richter, B and Mörgelin, Matthias and Perez, Maria Thereza and Su, W D and Chiquet-Ehrismann, R and Rauch, Uwe and Fässler, Reinhard},
  issn         = {0021-9525},
  keyword      = {epidermal growth factor,pair rule,ten-m/odz,transmembrane protein},
  language     = {eng},
  number       = {3},
  pages        = {563--577},
  publisher    = {Rockefeller University Press},
  series       = {Journal of Cell Biology},
  title        = {Mouse ten-m/Odz is a new family of dimeric type II transmembrane proteins expressed in many tissues},
  volume       = {145},
  year         = {1999},
}