Editors' ChoiceBiochemistry

Feeling Tense

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Science Signaling  03 Feb 2009:
Vol. 2, Issue 56, pp. ec44
DOI: 10.1126/scisignal.256ec44

Transduction of force between the extracellular matrix and the cytoskeleton is important for cellular function (see the Perspective by Schwartz). Although there are models for how talin, a protein that links membrane integrins with the cytoskeleton, might transduce force, experimental evidence has been lacking. Now del Rio et al. show that stretching of talin at physiologically relevant forces exposes cryptic binding sites for vinculin, a focal adhesion protein that is activated by talin binding, leading to cytoskeletal reorganization. Dynamic adhesion of cells to their microenvironment via cell surface–bound integrins is important for cell spreading and migration. Friedland et al. found that integrins can be activated by tension generated between the internal cytoskeleton and a fibronectin-coated surface. Tension regulates the integrin-fibronectin interaction, which switches between a relaxed and tensioned state and activates an intracellular signaling pathway.

A. del Rio, R. Perez-Jimenez, R. Liu, P. Roca-Cusachs, J. M. Fernandez, M. P. Sheetz, Stretching single talin rod molecules activates vinculin binding. Science 323, 638–641 (2009). [Abstract] [Full Text]

J. C. Friedland, M. H. Lee, D. Boettiger, Mechanically activated integrin switch controls α5β1 function. Science 323, 642–644 (2009). [Abstract] [Full Text]

M. A. Schwartz, The force is with us. Science 323, 588–589 (2009). [Summary] [Full Text]

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