Direct molecular force measurements of multiple adhesive interactions between cadherin ectodomains

S. Sivasankar, W. Brieher, N. Lavrik, B. Gumbiner, D. Leckband

Research output: Contribution to journalArticle

Abstract

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.

Original languageEnglish (US)
Pages (from-to)11820-11824
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume96
Issue number21
DOIs
StatePublished - Oct 12 1999

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Cadherins
Adhesives
Proteins
Xenopus
Rupture

ASJC Scopus subject areas

  • General

Cite this

Direct molecular force measurements of multiple adhesive interactions between cadherin ectodomains. / Sivasankar, S.; Brieher, W.; Lavrik, N.; Gumbiner, B.; Leckband, D.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 96, No. 21, 12.10.1999, p. 11820-11824.

Research output: Contribution to journalArticle

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