TY - JOUR AB - Although the relevance of mechanotransduction in cell signaling is currently appreciated, the mechanisms that drive this process remain largely unknown. Mechanical unfolding of proteins may trigger distinct downstream signals in cells, providing a mechanism for cellular mechanotransduction. Force-induced unfolding of talin, a prominent focal adhesion protein, has been demonstrated previously for a small portion of its rod domain. Here, using single-molecule atomic force microscopy (smAFM), we show that the entire talin rod can be unfolded by mechanical extension, over a physiological range of forces between 10 and 40 pN. We also demonstrate, through a combination of smAFM and steered molecular dynamics, that the different bundles within the talin rod exhibit a distinct hierarchy of mechanical stability. These results provide a mechanism by which different force conditions within the cell control a graduated unfolding of the talin rod. Mechanical unfolding of the rod subdomains, and the subsequent effect on talin’s binding interactions, would allow for a finely tuned cellular response to internally or externally applied forces. AU - Haining,AW AU - von,Essen M AU - Attwood,SJ AU - Hytonen,VP AU - del,Rio Hernandez A DO - 10.1021/acsnano.6b01658 EP - 6658 PY - 2016/// SN - 1936-0851 SP - 6648 TI - All subdomains of the talin rod are mechanically vulnerable and may contribute to cellular mechanosensing T2 - ACS Nano UR - http://dx.doi.org/10.1021/acsnano.6b01658 UR - https://pubs.acs.org/doi/10.1021/acsnano.6b01658 UR - http://hdl.handle.net/10044/1/34462 VL - 10 ER -