Actin filament assembly

Source: http://www.mechanobio.info/modules/go-0030041 (Mechanobiology Institute, Singapore). The actin network is made up of filamentous actin (F-actin). These filaments are highly dynamic in nature and comprise monomers of G-actin bound to either ATP (yellow) or ADP (blue). Assembly is powered by ATP hydrolysis and filament nucleation happens spontaneously in vitro. Polymerization: Addition of ATP-actin occurs at the barbed end, leading to filament elongation. Elongation will continue whilst the rate of elongation is greater than the loss of ADP-actin from the pointed end. Profilin preferentially binds to ATP-actin, inhibits nucleation and accelerates filament elongation in vivo. Depolymerization: When the dissociation rate of ADP-actin exceeds the rate of ATP-actin association, the filament shrinks. In vivo, this is aided by cofilin, which can severe filaments into short fragments and promote subunit loss from the pointed ends. Actin treadmilling occurs when the rate of association of ATP-actin and the rate of loss of ADP-actin are balanced.

Related links:
Filament Polarity: http://www.mechanobio.info/topics/cytoskeleton-dynamics/go-0005856/go-0005884

Capping Protein: http://www.mechanobio.info/Home/glossary-of-terms/mechano-glossary--a/capping-protein

Actin Nucleation: http://www.mechanobio.info/modules/go-0045010

Видео Actin filament assembly канала Mechanobiology Institute, Singapore