This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Chia, I. V.
Right arrow Articles by Costantini, F.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Chia, I. V.
Right arrow Articles by Costantini, F.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, June 2005, p. 4371-4376, Vol. 25, No. 11
0270-7306/05/$08.00+0     doi:10.1128/MCB.25.11.4371-4376.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Mouse Axin and Axin2/Conductin Proteins Are Functionally Equivalent In Vivo

Ian V. Chia and Frank Costantini*

Department of Genetics and Development, Columbia University Medical Center, 701 W. 168th Street, New York, New York 10032

Received 18 January 2005/ Returned for modification 24 February 2005/ Accepted 2 March 2005

Axin is a central component of the canonical Wnt signal transduction machinery, serving as a scaffold for the ß-catenin destruction complex. The related protein Axin2/Conductin, although less extensively studied, is thought to perform similar functions. Loss of Axin causes early embryonic lethality, while Axin2-null mice are viable but have craniofacial defects. Mutations in either gene contribute to cancer in humans. The lack of redundancy between Axin and Axin2 could be due to their different modes of expression: while Axin is expressed ubiquitously, Axin2 is expressed in tissue- and developmental-stage-specific patterns, and its transcription is induced by canonical Wnt signaling. Alternatively, the two proteins might have partially different functions, a hypothesis supported by the observation that they differ in their subcellular localizations in colon epithelial cells. To test the functional equivalence of Axin and Axin2 in vivo, we generated knockin mice in which the Axin gene was replaced with Myc-tagged Axin or Axin2 cDNA. Mice homozygous for the resulting alleles, AxinAx or AxinAx2, express no endogenous Axin but express either Myc-Axin or Myc-Axin2 under the control of the Axin locus. Both AxinAx/Ax and AxinAx2/Ax2 homozygotes are apparently normal and fertile, demonstrating that the Axin and Axin2 proteins are functionally equivalent.


* Corresponding author. Mailing address: Department of Genetics and Development, Columbia University Medical Center, 701 W. 168th Street, New York, NY 10032. Phone: (212) 305-6814. Fax: (212) 923-2090. E-mail: fdc3{at}columbia.edu.


Molecular and Cellular Biology, June 2005, p. 4371-4376, Vol. 25, No. 11
0022-538X/05/$08.00+0     doi:10.1128/MCB.25.11.4371-4376.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:

  • Yan, Y., Tang, D., Chen, M., Huang, J., Xie, R., Jonason, J. H., Tan, X., Hou, W., Reynolds, D., Hsu, W., Harris, S. E., Puzas, J. E., Awad, H., O'Keefe, R. J., Boyce, B. F., Chen, D. (2009). Axin2 controls bone remodeling through the {beta}-catenin-BMP signaling pathway in adult mice. J. Cell Sci. 122: 3566-3578 [Abstract] [Full Text]  
  • Cadigan, K. M., Peifer, M. (2009). Wnt Signaling from Development to Disease: Insights from Model Systems. Cold Spring Harb. Perspect. Biol. 1: a002881-a002881 [Abstract] [Full Text]  
  • Yang, H., Youm, Y.-H., Sun, Y., Rim, J.-S., Galban, C. J., Vandanmagsar, B., Dixit, V. D. (2009). Axin expression in thymic stromal cells contributes to an age-related increase in thymic adiposity and is associated with reduced thymopoiesis independently of ghrelin signaling. J. Leukoc. Biol. 85: 928-938 [Abstract] [Full Text]  
  • Chia, I. V., Kim, M. J., Itoh, K., Sokol, S. Y., Costantini, F. (2009). Both the RGS Domain and the Six C-Terminal Amino Acids of Mouse Axin Are Required for Normal Embryogenesis. Genetics 181: 1359-1368 [Abstract] [Full Text]  
  • Chen, T., Li, M., Ding, Y., Zhang, L.-s., Xi, Y., Pan, W.-j., Tao, D.-l., Wang, J.-y., Li, L. (2009). Identification of Zinc-finger BED Domain-containing 3 (Zbed3) as a Novel Axin-interacting Protein That Activates Wnt/{beta}-Catenin Signaling. J. Biol. Chem. 284: 6683-6689 [Abstract] [Full Text]  
  • Kim, M. J., Chia, I. V., Costantini, F. (2008). SUMOylation target sites at the C terminus protect Axin from ubiquitination and confer protein stability. FASEB J. 22: 3785-3794 [Abstract] [Full Text]  
  • Wang, X., Goode, E. L., Fredericksen, Z. S., Vierkant, R. A., Pankratz, V. S., Liu-Mares, W., Rider, D. N., Vachon, C. M., Cerhan, J. R., Olson, J. E., Couch, F. J. (2008). Association of Genetic Variation in Genes Implicated in the {beta}-Catenin Destruction Complex with Risk of Breast Cancer. Cancer Epidemiol. Biomarkers Prev. 17: 2101-2108 [Abstract] [Full Text]  
  • Zeng, X., Huang, H., Tamai, K., Zhang, X., Harada, Y., Yokota, C., Almeida, K., Wang, J., Doble, B., Woodgett, J., Wynshaw-Boris, A., Hsieh, J.-C., He, X. (2008). Initiation of Wnt signaling: control of Wnt coreceptor Lrp6 phosphorylation/activation via frizzled, dishevelled and axin functions. Development 135: 367-375 [Abstract] [Full Text]  
  • Zhang, S., Cagatay, T., Amanai, M., Zhang, M., Kline, J., Castrillon, D. H., Ashfaq, R., Oz, O. K., Wharton, K. A. Jr. (2007). Viable Mice with Compound Mutations in the Wnt/Dvl Pathway Antagonists nkd1 and nkd2. Mol. Cell. Biol. 27: 4454-4464 [Abstract] [Full Text]