Please use this identifier to cite or link to this item: https://doi.org/10.1126/science.1162912
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dc.titleStretching single talin rod molecules activates vinculin binding
dc.contributor.authorDel Rio, A.
dc.contributor.authorPerez-Jimenez, R.
dc.contributor.authorLiu, R.
dc.contributor.authorRoca-Cusachs, P.
dc.contributor.authorFernandez, J.M.
dc.contributor.authorSheetz, M.P.
dc.date.accessioned2014-10-16T09:42:15Z
dc.date.available2014-10-16T09:42:15Z
dc.date.issued2009-01-30
dc.identifier.citationDel Rio, A., Perez-Jimenez, R., Liu, R., Roca-Cusachs, P., Fernandez, J.M., Sheetz, M.P. (2009-01-30). Stretching single talin rod molecules activates vinculin binding. Science 323 (5914) : 638-641. ScholarBank@NUS Repository. https://doi.org/10.1126/science.1162912
dc.identifier.issn00368075
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/98037
dc.description.abstractThe molecular mechanism by which a mechanical stimulus is translated into a chemical response in biological systems is still unclear. We show that mechanical stretching of single cytoplasmic proteins can activate binding of other molecules. We used magnetic tweezers, total internal reflection fluorescence, and atomic force microscopy to investigate the effect of force on the interaction between talin, a protein that links liganded membrane integrins to the cytoskeleton, and vinculin, a focal adhesion protein that is activated by talin binding, leading to reorganization of the cytoskeleton. Application of physiologically relevant forces caused stretching of single talin rods that exposed cryptic binding sites for vinculin. Thus in the talin-vinculin system, molecular mechanotransduction can occur by protein binding after exposure of buried binding sites in the talin-vinculin system. Such protein stretching may be a more general mechanism for force transduction.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1126/science.1162912
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentPHYSICS
dc.description.doi10.1126/science.1162912
dc.description.sourcetitleScience
dc.description.volume323
dc.description.issue5914
dc.description.page638-641
dc.description.codenSCIEA
dc.identifier.isiut000262862800044
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