Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.bbrc.2007.08.096
Title: Molecular force spectroscopy of homophilic nectin-1 interactions
Authors: Vedula, S.R.K. 
Lim, T.S.
Hui, S.
Kausalya, P.J.
Lane, E.B.
Rajagopal, G.
Hunziker, W.
Lim, C.T. 
Keywords: Cell adhesion
Nectins
Single-molecule force spectroscopy
Issue Date: 3-Nov-2007
Citation: Vedula, S.R.K., Lim, T.S., Hui, S., Kausalya, P.J., Lane, E.B., Rajagopal, G., Hunziker, W., Lim, C.T. (2007-11-03). Molecular force spectroscopy of homophilic nectin-1 interactions. Biochemical and Biophysical Research Communications 362 (4) : 886-892. ScholarBank@NUS Repository. https://doi.org/10.1016/j.bbrc.2007.08.096
Abstract: Nectins are Ca2+ independent cell adhesion molecules localizing at the cadherin based adherens junctions. In this study, we have used atomic force microscopy to study interaction of a chimera of extra cellular fragment of nectin-1 and Fc of human IgG (nef-1) with wild type L-fibroblasts that express endogenous nectin-1 to elucidate the biophysical characteristics of homophilic nectin-1 trans-interactions at the level of single molecule. Bond strength distribution revealed three distinct bound states (or configurations) of trans-interactions between paired nectins, where each bound state has a unique unstressed off-rate and reactive compliance. Kinetic analysis of force-dependent off-rate of the bound state involving trans-interacting V-V domains between paired nectin-1 (unstressed off-rate ∼1.465 ± 0.779 s-1, reactive compliance ∼0.143 ± 0.072 nm) was found to be closest to E-cadherin, indicating that V-V domain trans-interactions are probably necessary to initiate and promote adhesions of E-cadherin at adherens junctions (AJs). © 2007 Elsevier Inc. All rights reserved.
Source Title: Biochemical and Biophysical Research Communications
URI: http://scholarbank.nus.edu.sg/handle/10635/85433
ISSN: 0006291X
DOI: 10.1016/j.bbrc.2007.08.096
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