Myosin assembly/polymerization

Just as myosins are able to move along microfilaments, there are motor proteins that move along microtubules. Microtubules, like microfilaments, are polar polymeric assemblies, but unlike actin-myosin interactions, microtubule-based motors exist that move along microtubules in either direction. A constant traffic of vesicles and organelles is visible in cultured cells especially using time-lapse photography. The larger part of this movement takes place on micrombules and is stimulated by phorbol ester (an activator of protein kinase C), and over-expression of N-J aj oncoprotein (Alexandrova et al., 1993). 

Actin, the major constituent of the thin filaments, exists in two forms. In solutions of low ionic strength it exists as a 42kDa monomer, termed G-actin because of its globular shape. As the ionic strength of the solution rises to that at the physiological level, G-actin polymerizes into a fibrous form, F-actin, that resembles the thin filaments found in muscle. Although actin, like myosin, is an ATPase, the hydrolysis of ATP is not involved in the contraction-relaxation cycle of muscle but rather in the assembly and disassembly of the actin filament. 

Myosins, kinesins, and dyneins move by cycling between states with different affinities for the long, polymeric macromolecules that serve as their tracks. For myosin, the molecular track is a polymeric form of actin, a 42-kd protein that is one of the most abundant proteins in eukaryotic cells, typically accounting for as much as 10% of the total protein. Actin polymers are continually being assembled and disassembled in cells in a highly dynamic manner, accompanied by the hydrolysis of ATP. On the microscopic scale, actin filaments participate in the dynamic reshaping of the cytoskeleton and the cell itself and in other motility mechanisms that do not include myosin. In muscle, myosin and actin together are the key components responsible for muscle contraction. 

Kinetic studies have shown that filament initiation is more difficult than subsequent elongation (Cross et al., 1991). In a system where assembly-disassembly might play a large role, for example, in nonmuscle vertebrate cells, this property predicts that the rate at which monomers become available for polymerization could alter both the number and length of myosin filaments that are formed. Thus control of kinase activity, which controls the number of assembly competent extended monomers, could be a factor in determining subsequent polymerization. 

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