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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Items 101–119 of 119
Effects of FSGS-associated mutations on the stability and function of myosin-1 in fission yeast
Bi‐Karchin, J., Carroll, R. T., James, M. L., et al. (2015) · Disease Models & Mechanisms · doi:10.1242/dmm.020214 · Cited by 3
“Unlike kinesins, ATP-bound myosins exhibit weak binding to actin filaments (Hackney, 1996).”
BackgroundMyosin and kinesin: mother and child reunited
Hackney, D. D. (1996) · Chemistry & Biology · doi:10.1016/s1074-5521(96)90142-8 · Cited by 3
Self-citationZhang, Y., Liang, F., Xu, C., Warren, A., & Li, L. (2025) · European Journal of Protistology · doi:10.1016/j.ejop.2025.126167 · Cited by 2
Herman, I. P. (2016) · Biological and medical physics, biomedical engineering · doi:10.1007/978-3-319-23932-3_5 · Cited by 1
Communication between DNA and nucleotide binding sites facilitates stepping by the RecBCD helicase
Gaydar, V., Zananiri, R., Saied, L., et al. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae108 · Cited by 1
“The bound nucleotide state (ATP, ADP×Pi, or ADP) modulates the motor affinities towards the lattice it transverse on, as has been shown for all myosins, kinesin as well as for some helicases [16-20].”
BackgroundMolecular Machines in 3D and 2D Systems: Movement, Mechanical Work, and Switching. A Review
Kutsybala, D. S., Shokurov, A. V., & Selektor, S. L. (2021) · Protection of Metals and Physical Chemistry of Surfaces · doi:10.1134/s2070205121050154 · Cited by 1
Motor proteins of the kinesin superfamily
Hackney, D. D. (2003) · The Enzymes · doi:10.1016/s1874-6047(04)80004-0 · Cited by 1
Self-citationKinetic and statistical mechanical modeling of DNA unzipping and kinesin mechanochemistry
Herskowitz, L. (2011) · UNM’s Digital Repository (University of New Mexico) · Cited by 1
Nature‐Inspired Molecular Machines
Lawit, A., Juluri, B. K., & Huang, T. J. (2010) · Nanotechnologies for the Life Sciences · doi:10.1002/9783527610419.ntls0206
Huang, T. J. (2008) · Elsevier eBooks · doi:10.1016/b978-044452190-3.00052-5
Aspects of Modeling Transport in Small Systems with a Look at Motor Proteins
Kinderlehrer, D. S. (2007) · Springer eBooks · doi:10.1007/978-3-540-74339-2_9
“Hackney [ 8 ]. The methods described here may be elaborated to include some additional features, even without incorporating multiple reaction coordinates, for example.”
MethodSmall-Molecule Control of Kinesin-5 Proteins
Learman, S. S. (2008) · VTechWorks (Virginia Tech)
Communication between DNA and nucleotide binding sites facilitates stepping by the RecBCD helicasePreprint
Gaydar, V., Zananiri, R., Dvir, O., et al. (2017) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/190215
Cartelli, D. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-818000-6.00006-8
(2010) · Calcium binding proteins · doi:10.1002/9780470872390.refs
Goldman, Y. E. (2003) · The Enzymes · doi:10.1016/s1874-6047(04)80002-7
Introduction to Stochastic Kinetic Models for Molecular Motors
Mugnai, M. L., Takaki, R., & Thirumalai, D. (2022) · Graduate texts in physics · doi:10.1007/978-3-030-98606-3_5
Colour change, origin of new species? The chameleon case
Dollion, A. Y. (2019) · theses.fr (ABES) · doi:10.70675/d10c9bc6z13acz4ad5z9379z95e18b1a78a6
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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