The kinetic cycles of myosin, kinesin, and dynein

Hackney, D D

doi:10.1146/annurev.ph.58.030196.003503

Cited by 119Microtubule and mitosis dynamicsCardiomyopathy and Myosin StudiesProtein Structure and Dynamics

The kinetic cycles of myosin, kinesin, and dynein

Hackney, D D·1996·Annual Review of Physiology

DOI 10.1146/annurev.ph.58.030196.003503

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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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Binding of native kinesin to MTs is too weak in the presence of ATP to maintain the sustained contact required for processive motion.
“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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Kinesin-1, -2, and -3 motors use family-specific mechanochemical strategies to effectively compete with dynein during bidirectional transport
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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
DOI: 10.1146/annurev.ph.58.030196.003503
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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The kinetic cycles of myosin, kinesin, and dynein

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