Simultaneous growth and breakdown on opposite ends of a protein filament
Actin Treadmilling Mechanism. This figure assumes that the critical concentration at the positive end is less than the critical concentration at the negative end and that the cytosolic subunit concentration is in between the positive and negative end critical concentrations.
In molecular biology, treadmilling is a phenomenon observed within protein filaments of the cytoskeletons of many cells, especially in actin filaments and microtubules. It occurs when one end of a filament grows in length while the other end shrinks, resulting in a section of filament seemingly "moving" across a stratum or the cytosol. This is due to the constant removal of the protein subunits from these filaments at one end of the filament, while protein subunits are constantly added at the other end.[1] Treadmilling was discovered by Wegner,[2] who defined the thermodynamic and kinetic constraints. Wegner recognized that: “The equilibrium constant (K) for association of a monomer with a polymer is the same at both ends, since the addition of a monomer to each end leads to the same polymer.”; a simple reversible polymer can’t treadmill; ATP hydrolysis is required. GTP is hydrolyzed for microtubule treadmilling.
^Bruce Alberts, Dennis Bray, Julian Lewis: Molecular Biology of the Cell, 4th Edition, Taylor & Francis, 2002, pp. 909-920, ISBN 0-8153-4072-9
^Wegner, A (Nov 1976). "Head to tail polymerization of actin". J Mol Biol. 108 (1): 139–150. doi:10.1016/S0022-2836(76)80100-3. PMID 1003481.
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