The roles of ATP in the dynamics of the actin filaments of the cytoskeleton

In contrast to the actin filaments of muscle, which are stabilized by special proteins, actin filaments of the cytoskeleton are highly dynamic. In vitro observations at room temperature have led to the conclusion that the hydrolysis of ATP, which accompanies the polymerization of ATP-containing monomers, destabilizes the filaments of the actin skeleton. Many functions of this skeleton, such as signal transduction, the anchoring of cell adhesion complexes, and the transfer and generation of pulling forces, can obviously only be adequately performed by stable filaments. Here it is assumed that, at room temperature, the interaction of ADP-containing monomers is impaired by complexed water molecules that partly shield the binding surfaces. The possibility that, at higher temperatures, the interaction of the monomers is strong enough to prevent spontaneous filament depolymerization is explored. Using mechanical models that take into account binding forces and energies, the polymerization cycle expected under these conditions is described. It is shown that ATP serves primarily to prevent incorrect binding of the incoming monomer to the end of the filament ('adjusted fit'). In addition, it provides the free energy needed for disassembly of the expected stable filaments.