The DOI matches its Crossref record.
The Kinetic Cycles of Myosin, Kinesin, and Dynein
Abstract
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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“Finally, binding of native kinesin to MTs is too weak in the presence of ATP to maintain the sustained contact required for processive motion (Vale et al., 1985; Hackney, 1996).”
From Light Chain– dependent Regulation of Kinesin's Interaction with Microtubules (1998) · cites this paper as Hackney, 1996
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THE ATP SYNTHASE—A SPLENDID MOLECULAR MACHINE
Boyer, P. D. (1997) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.66.1.717 · Cited by 2,014
Kinesin and Dynein Superfamily Proteins and the Mechanism of Organelle Transport
Hirokawa, N. (1998) · Science · doi:10.1126/science.279.5350.519 · Cited by 1,689
The Way Things Move: Looking Under the Hood of Molecular Motor Proteins
Vale, R. D., & Milligan, R. A. (2000) · Science · doi:10.1126/science.288.5463.88 · Cited by 1,503
Dynactin increases the processivity of the cytoplasmic dynein motor
King, S. J., & Schroer, T. A. (1999) · Nature Cell Biology · doi:10.1038/71338 · Cited by 661
“Cytoplasmic dynein, another microtubule-based motor, has been intractable for in vitro single-molecule studies because of its large size, complex polypeptide composition and ATPase kinetics (reviewed i”
BackgroundCytoplasmic dynein functions as a gear in response to load
Mallik, R., Carter, B. C., Lex, S. A., King, S. J., & Gross, S. P. (2004) · Nature · doi:10.1038/nature02293 · Cited by 494
“These ‘nanomachines’ use energy obtained from ATP hydrolysis to generate forc”
Background
Metadata
- Authors
- Hackney, D. D.
- Affiliations
- Carnegie Mellon University (US)
- Corresponding author
- Hackney, D D
- ORCID
- Hackney, D D
- Venue
- Annual Review of Physiology
- Publisher
- Annual Reviews
- Published
- 1996-10
- Volume
- 58
- Issue
- 1
- Pages
- 731-750
- ISSN
- 0066-4278 (ISSN-L)
- 1545-1585
- OpenAlex
- W2085849675
- Cited by
- 118
- References
- 0
- Citations by year
- 2025: 2 · 2024: 2 · 2023: 1 · 2022: 3 · 2021: 3 · 2020: 1 · 2019: 3 · 2018: 1 · 2016: 3 · 2015: 1 · 2014: 2 · 2013: 1 · 2012: 2
- FWCI
- 4.33
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Annual Review of Physiology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Cardiomyopathy and Myosin Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- myosin, kinesin, dynein, molecular motors, ATPase cycle, ATP hydrolysis, F-actin, microtubules, processive movement, muscle contraction, organelle movement, cytokinesis
- MeSH terms
- Adenosine Triphosphatases, Animals, Dyneins, Humans, Kinetics, Muscle Contraction, Muscles, Myosins, Kinesins
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