The non-equilibrium thermodynamics and kinetics of focal adhesion dynamics.

ABSTRACT:

Background

We consider a focal adhesion to be made up of molecular complexes, each consisting of a ligand, an integrin molecule, and associated plaque proteins. Free energy changes drive the binding and unbinding of these complexes and thereby controls the focal adhesion's dynamic modes of growth, treadmilling and resorption.

Principal findings

We have identified a competition among four thermodynamic driving forces for focal adhesion dynamics: (i) the work done during the addition of a single molecular complex of a certain size, (ii) the chemical free energy change associated with the addition of a molecular complex, (iii) the elastic free energy change associated with deformation of focal adhesions and the cell membrane, and (iv) the work done on a molecular conformational

SUBMITTER: Olberding JE 

PROVIDER: S-EPMC2923603 | biostudies-literature | 2010 Aug

REPOSITORIES: biostudies-literature