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Title: Remarkable disparity in mechanical response among the extracellular domains of type i and II cadherins
Authors: Liu, R. 
Wu, F.
Thiery, J.P. 
Keywords: AFM force mode
calcium bridge
cell adhesion
classical type I cadherins
classical type II cadherins
conformational dynamics
homophilic interaction
intermediate state
single-molecule force spectroscopy
SMD simulation
Issue Date: 1-Oct-2013
Citation: Liu, R., Wu, F., Thiery, J.P. (2013-10-01). Remarkable disparity in mechanical response among the extracellular domains of type i and II cadherins. Journal of Biomolecular Structure and Dynamics 31 (10) : 1137-1149. ScholarBank@NUS Repository.
Abstract: Cadherins, a large family of calcium-dependent adhesion molecules, are critical for intercellular adhesion. While crystallographic structures for several cadherins show clear structural similarities, their relevant adhesive strengths vary and their mechanisms of adhesion between types I and II cadherin subfamilies are still unclear. Here, stretching of cadherins was explored experimentally by atomic force microscopy and computationally by steered molecular dynamics (SMD) simulations, where partial unfolding of the E-cadherin ectodomains was observed. The SMD simulations on strand-swapping cadherin dimers displayed similarity in binding strength, suggesting contributions of other mechanisms to explain the strength differences of cell adhesion in vivo. Systematic simulations on the unfolding of the extracellular domains of type I and II cadherins revealed diverse pathways. However, at the earliest stage, a remarkable similarity in unfolding was observed for the various type I cadherins that was distinct from that for type II cadherins. This likely correlates positively with their distinct adhesive properties, suggesting that the initial forced deformation in type I cadherins may be involved in cadherin-mediated adhesion. © 2012 Taylor and Francis.
Source Title: Journal of Biomolecular Structure and Dynamics
ISSN: 07391102
DOI: 10.1080/07391102.2012.726530
Appears in Collections:Staff Publications

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