This review highlights the similarities and differences in the ATPase cycles of myosin, kinesin, and dynein, noting their shared burst kinetics and rate-limiting product release.
Provides framework for motor protein kinetics in muscle; leaves open targeted cardiovascular applications pending further study.
The ATPase cycles of the molecular motors myosin, kinesin, and dynein are reviewed, with emphasis on their similarities and differences. Myosin generates motility along actin filaments and functions in muscle contraction, organelle movement, and cytokinesis. Dynein and kinesin produce movement along microtubules. All the motors exhibit burst kinetics with rate-limiting product release. Binding of the products-complex to the filament accelerates product release and completes the ATPase cycle. Kinesin is able to generate processive movement, and the possibilities for how this could be generated by coupling to ATP hydrolysis are discussed.
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David D. Hackney (1996) studied this question.
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