Please use this identifier to cite or link to this item:
|Title:||Stretching single talin rod molecules activates vinculin binding|
|Authors:||Del Rio, A.|
|Source:||Del 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|
|Abstract:||The 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.|
|Appears in Collections:||Staff Publications|
Show full item record
Files in This Item:
There are no files associated with this item.
checked on Feb 7, 2018
WEB OF SCIENCETM
checked on Jan 31, 2018
checked on Feb 19, 2018
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.