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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 |
Appears in Collections: | Staff Publications |
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