Dissecting subsecond cadherin bound states reveals an efficient way for cells to achieve ultrafast probing of their environment

Anne Pierres, Anil Prakasam, Dominique Touchard, Anne Marie Benoliel, Pierre Bongrand, Deborah E Leckband

Research output: Contribution to journalArticle


Cells continuously probe their environment with membrane receptors, achieving subsecond adaptation of their behaviour [Diez, G., Gerisch, G., Anderson, K., Müller-Taubenberger, A. and Bretschneider, T. (2006) Subsecond reorganization of the actin network in cell motility and chemotaxis. Proc. Natl. Acad. Sci. USA 102, 7601-7606, Shamri, R., Grabovsky, V., Gauguet, J.M., Feigelson, S., Manevich, E., Kolanus, W., Robinson, M.K., Staunton, D.E., von Andrian, U.H. and Alon, R. (2005) Lymphocyte arrest requires instantaneous induction of an extended LFA-1 conformation mediated by endothelium-bound chemokines. Nat. Immunol. 6, 497-606, Jiang, G., Huang, A.H., Cai, Y., Tanase, M. and Sheetz, M.P. (2006) Rigidity sensing at the leading edge through αVβ3 integrins and RPTPα. Biophys. J. 90, 1804-2006]. Recently, several receptors, including cadherins, were found to bind ligands with a lifetime of order of one second. Here we show at the single molecule level that homotypic C-cadherin association involves transient intermediates lasting less than a few tens of milliseconds. Further, these intermediates transitionned towards more stable states with a kinetic rate displaying exponential decrease with piconewton forces. These features enable cells to detect ligands or measure surrounding mechanical behaviour within a fraction of a second, much more rapidly than was previously thought.

Original languageEnglish (US)
Pages (from-to)1841-1846
Number of pages6
JournalFEBS Letters
Issue number9
StatePublished - May 1 2007



  • Binding kinetics
  • Cadherins
  • Flow chamber
  • Molecular forces

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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