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On the Molecular Basis for Mechanotransduction

Roger D. Kamm1,1,2,2, Mohammad R. Kaazempur-Mofrad1,1

Department of Mechanical Engineering and Biological Engineering Division Massachusetts Institute of Technology Cambridge, MA 02139 - USA
500 Technology Square Room NE47-315Cambridge, MA 02139Phone: (617) 253-5330 Fax: (617) 258-5239E-mail:

Molecular & Cellular Biomechanics 2004, 1(3), 201-210.


Much is currently known about the signaling pathways that are excited when cells are subjected to a mechanical stimulus, yet we understand little of the process by which the mechanical perturbation is transformed into a biochemical signal. Numerous theories have been proposed, and each has merit. While cells may possess many different ways of responding to stress, the existence of a single unifying principle has much appeal. Here we propose the hypothesis that cells sense mechanical force through changes in protein conformation, leading to altered binding affinities of proteins, ultimately initiating an intracellular signaling cascade or producing changes in the proteins localized to regions of high stress. More generally, this represents an alternative to transmembrane signaling through receptor-ligand interactions providing the cell with a means of reacting to changes in its mechanical, as opposed to biochemical, environment. One example is presented showing how the binding affinity between the focal adhesion targeting domain of focal adhesion kinase and the LD motif of paxillin is influenced by externally applied force.

Cite This Article

Kamm, R. D., Kaazempur-Mofrad, M. R. (2004). On the Molecular Basis for Mechanotransduction. Molecular & Cellular Biomechanics, 1(3), 201–210.

cc This work is licensed under a Creative Commons Attribution 4.0 International License , which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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