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 Troyanovsky, R. B.
Right arrow Articles by Troyanovsky, S. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Troyanovsky, R. B.
Right arrow Articles by Troyanovsky, S. M.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, November 2003, p. 7965-7972, Vol. 23, No. 22
0270-7306/03/$08.00+0     DOI: 10.1128/MCB.23.22.7965-7972.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Adhesive and Lateral E-Cadherin Dimers Are Mediated by the Same Interface

Regina B. Troyanovsky, Eugene Sokolov, and Sergey M. Troyanovsky*

Division of Dermatology, Washington University Medical School, St. Louis, Missouri 63110

Received 28 April 2003/ Returned for modification 21 July 2003/ Accepted 4 August 2003

E-cadherin is a transmembrane protein that mediates Ca2+-dependent cell-cell adhesion. To study cadherin-cadherin interactions that may underlie the adhesive process, a recombinant E-cadherin lacking free sulfhydryl groups and its mutants with novel cysteines were expressed in epithelial A-431 cells. These cysteine mutants, designed according to various structural models of cadherin dimers, were constructed to reveal cadherin dimerization by the bifunctional sulfhydryl-specific cross-linker BM[PE0]3. Cross-linking experiments with the mutants containing a cysteine at strand B of their EC1 domains did show cadherin dimerization. By their properties these dimers correspond to those which have been characterized by coimmunoprecipitation assay. Under standard culture conditions the adhesive dimer is a dominant form. Calcium depletion dissociates adhesive dimers and promotes the formation of lateral dimers. Our data show that both dimers are mediated by the amino-terminal cadherin domain. Furthermore, the interfaces involved in both adhesive and lateral dimerization appear to be the same. The coexistence of the structurally identical adhesive and lateral dimers suggests some flexibility of the extracellular cadherin region.

* Corresponding author. Mailing address: Division of Dermatology, Washington University Medical School, Campus Box 8123, 660 S. Euclid Ave., St. Louis, MO 63110. Phone: (314) 362-8154. Fax: (314) 362-8159. E-mail: sergeyt{at}im.wustl.edu.

Molecular and Cellular Biology, November 2003, p. 7965-7972, Vol. 23, No. 22
0022-538X/03/$08.00+0     DOI: 10.1128/MCB.23.22.7965-7972.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • de Beco, S., Gueudry, C., Amblard, F., Coscoy, S. (2009). Endocytosis is required for E-cadherin redistribution at mature adherens junctions. Proc. Natl. Acad. Sci. USA 106: 7010-7015 [Abstract] [Full Text]  
  • Zhang, Y., Sivasankar, S., Nelson, W. J., Chu, S. (2009). Resolving cadherin interactions and binding cooperativity at the single-molecule level. Proc. Natl. Acad. Sci. USA 106: 109-114 [Abstract] [Full Text]  
  • Kiss, A., Troyanovsky, R. B., Troyanovsky, S. M. (2008). p120-Catenin Is a Key Component of the Cadherin-{gamma}-Secretase Supercomplex. Mol. Biol. Cell 19: 4042-4050 [Abstract] [Full Text]  
  • Salim, A., Ratner, L. (2008). Modulation of {beta}-Catenin and E-Cadherin Interaction by Vpu Increases Human Immunodeficiency Virus Type 1 Particle Release. J. Virol. 82: 3932-3938 [Abstract] [Full Text]  
  • Tsuiji, H., Xu, L., Schwartz, K., Gumbiner, B. M. (2007). Cadherin Conformations Associated with Dimerization and Adhesion. J. Biol. Chem. 282: 12871-12882 [Abstract] [Full Text]  
  • Yonekura, S., Ting, C.-Y., Neves, G., Hung, K., Hsu, S.-n., Chiba, A., Chess, A., Lee, C.-H. (2006). The Variable Transmembrane Domain of Drosophila N-Cadherin Regulates Adhesive Activity.. Mol. Cell. Biol. 26: 6598-6608 [Abstract] [Full Text]  
  • Troyanovsky, R. B., Sokolov, E. P., Troyanovsky, S. M. (2006). Endocytosis of Cadherin from Intracellular Junctions Is the Driving Force for Cadherin Adhesive Dimer Disassembly. Mol. Biol. Cell 17: 3484-3493 [Abstract] [Full Text]  
  • Chu, Y.-S., Eder, O., Thomas, W. A., Simcha, I., Pincet, F., Ben-Ze'ev, A., Perez, E., Thiery, J. P., Dufour, S. (2006). Prototypical Type I E-cadherin and Type II Cadherin-7 Mediate Very Distinct Adhesiveness through Their Extracellular Domains. J. Biol. Chem. 281: 2901-2910 [Abstract] [Full Text]  
  • Thoumine, O., Lambert, M., Mege, R.-M., Choquet, D. (2006). Regulation of N-Cadherin Dynamics at Neuronal Contacts by Ligand Binding and Cytoskeletal Coupling. Mol. Biol. Cell 17: 862-875 [Abstract] [Full Text]  
  • Garrod, D. R., Berika, M. Y., Bardsley, W. F., Holmes, D., Tabernero, L. (2005). Hyper-adhesion in desmosomes: its regulation in wound healing and possible relationship to cadherin crystal structure. J. Cell Sci. 118: 5743-5754 [Abstract] [Full Text]  
  • Harrison, O. J., Corps, E. M., Berge, T., Kilshaw, P. J. (2005). The mechanism of cell adhesion by classical cadherins: the role of domain 1. J. Cell Sci. 118: 711-721 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»