Direct Molecular Force Measurements of Multiple Adhesive Interactions between Cadherin Ectodomains

Direct-force measurements of the interactions between recombinant C-cadherin from Xenopus demonstrated that the ectodomain of cadherin exhibits multiple adhesive contacts that involve successive domains along the extracellular region of the protein. Contacts between the fully interdigitated antipara...

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Published inProceedings of the National Academy of Sciences - PNAS Vol. 96; no. 21; pp. 11820 - 11824
Main Authors Sivasankar, S., Brieher, W., Lavrik, N., Gumbiner, B., Leckband, D.
Format Journal Article
LanguageEnglish
Published United States National Academy of Sciences of the United States of America 12.10.1999
National Acad Sciences
The National Academy of Sciences
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Summary:Direct-force measurements of the interactions between recombinant C-cadherin from Xenopus demonstrated that the ectodomain of cadherin exhibits multiple adhesive contacts that involve successive domains along the extracellular region of the protein. Contacts between the fully interdigitated antiparallel proteins form the strongest adhesive interaction. A second weaker minimum was measured when the interdigitated proteins were separated by a distance equal to the length of one domain of the extracellular (EC) fragment and corresponding to the antiparallel alignment of domains one through four (EC1 through EC4). The successive rupture of these interactions generates an unbinding force profile that may be optimized to impede the abrupt failure of cadherin-mediated junctions under force.
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To whom reprint requests should be addressed. E-mail: leckband@uiuc.edu.
Communicated by William R. Schowalter, University of Illinois at Urbana-Champaign, Urbana, IL
Present address: Department of Cell Biology, Harvard Medical School, Longwood Avenue, Boston, MA 02115.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.96.21.11820