Fig. 3. Contribution of cellular tensegrity to mechanochemical transduction. (Top) A schematic diagram of the tensegrity-based complementary force balance between tensed microfilaments, compressed microtubules and transmembrane integrin receptors (gray oval dimer) in living cells (intermediate filaments are not shown for simplicity) (for details, see Ingber, 2003). Black forms indicate regulatory proteins and enzymes that are physically immobilized on load-bearing cytoskeletal filaments; red oval represents a transmembrane protein that does not link to the internal cytoskeletal lattice. (Bottom) When force is applied to integrins, thermodynamic and kinetic parameters change locally for cytoskeleton-associated molecules that physically experience the mechanical load; when force is applied to non-adhesion receptors that do not link to the cytoskeleton, stress dissipates locally at the cell surface, and the biochemical response is muted. In this diagram, new tubulin monomers add onto the end of a microtubule (yellow symbols) when tension is applied to integrins, and the microtubule is decompressed as a result of a change in the critical concentration of tubulin. The blue form indicates a molecule that is physically distorted by stress transferred from integrins to the cytoskeleton and, as a result, changes its kinetics (increases its rate constant for chemical conversion of substrate 1 into product 2). In this manner, both cytoskeletal structure (architecture) and prestress (tension) in the cytoskeleton may modulate the cellular response to mechanical stress.

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