Abstract
Living polymerization of the two major proteins in eucaryotic cells: actin and tubulin is reviewed. Actin is a large globular protein built of 375 alpha-amino acid residues and has a molecular weight of 42,000. It polymerizes in vivo and in vitro with the formation of long linear filaments (up to 50 microns) with two distinguished (“plus” and “minus”) ends. Actin filaments are in equilibrium with the surrounding monomeric actin and undergo treadmilling, i.e., continuous polymerization at the plus end and depolymerization at the minus end which allows their spacial movement without changing the filament length. Tubulin is a larger globular protein (dimer) with a molecular weight of 100,000 which exhibits similar polymerization behavior. Microtubulin filaments, however, characterize with dynamic instability, i.e., they polymerize slower but undergo very fast depolymerization. Cell utilization and regulation of actin and tubulin polymerization is briefly reviewed as well.
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Dirlikov, S. (1994). Living Polymerization of Proteins: Actin and Tubulin. A Review. In: Gebelein, C.G., Carraher, C.E. (eds) Biotechnology and Bioactive Polymers. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-9519-6_9
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DOI: https://doi.org/10.1007/978-1-4757-9519-6_9
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