Actin filaments and microtubules make up the principal dynamic constituents of the cytoskeleton. Actin is capable of entering into a variety of interactions with other proteins which regulate its state. The simplest possible in vitro system — that in which the actin monomers polymerize to form long linear aggregates — has been found to embody a number of properties reflecting the dynamics of the turnover of actin filaments in cells. Actin filaments can quickly polymerize and depolymerize, they can spontaneously break and associate end to end, and an ATPase activity causes actin filaments to “treadmill”, that is to polymerize at one end and to depolymerize simultaneously at the other end.
KeywordsActin Filament Actin Polymerization Actin Monomer Filament Length Linear Aggregate
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- 6.Lai, A. A., Korn, E. D. & Brenner, S. L. (1984) J. Biol. Chem. 259, 8794–8800.Google Scholar
- 10.Kondo, H. & Ishiwata, S. (1976) J. Biochem. (Tokyo) 79, 159–171.Google Scholar
- 11.earlier, M.-F., Pantaloni, D. & Korn, E. D. (1984) J. Biol. Chem. 259, 9987–9991.Google Scholar
- 15.Earlier, M.-F., Pantaloni, D. & Korn, E. D. (1984) J. Biol. Chem.259, 9983–9986.Google Scholar