Kinesin Assembly and Movement in Cells
Abstract
Long-distance transport in eukaryotic cells is driven by molecular motors that move along microtubule tracks. Molecular motors of the kinesin superfamily contain a kinesin motor domain attached to family-specific sequences for cargo binding, regulation, and oligomerization. The biochemical and biophysical properties of the kinesin motor domain have been widely studied, yet little is known about how kinesin motors work in the complex cellular environment. We discuss recent studies on the three major families involved in intracellular transport (kinesin-1, kinesin-2, and kinesin-3) that have begun to bridge the gap in knowledge between the in vitro and in vivo behaviors of kinesin motors. These studies have increased our understanding of how kinesin subunits assemble to produce a functional motor, how kinesin motors are affected by biochemical cues and obstacles present on cellular microtubules, and how multiple motors on a cargo surface can work collectively for increased force production and travel distance.
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Kinesin family members are a class of motor proteins involved in cell movements and intracellular vesicles' trafficking from ER, and in chromosome and centrosome positioning during mitosis.
“a class of motor proteins involved in cell movements and intracellular vesicles’ trafficking from ER, and in chromosome and centrosome positioning during mitosis [66]”
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Distinct conformations of the kinesin Unc104 neck regulate a monomer to dimer motor transition
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Molecular landmarks along the axonal route: axonal transport in health and disease
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To step or not to step? How biochemistry and mechanics influence processivity in Kinesin and Eg5
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Conventional Kinesin Holoenzymes Are Composed of Heavy and Light Chain Homodimers
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Conventional Kinesin Mediates Microtubule-Microtubule Interactions In Vivo
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Characterization of the Movement of the Kinesin Motor KIF1A in Living Cultured Neurons
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Characterization of α2β2 and α2 forms of kinesin
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KIF1D is a fast non‐processive kinesin that demonstrates novel K‐loop‐dependent mechanochemistry
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Dynactin Enhances the Processivity of Kinesin‐2
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Single-Molecule Behavior of Monomeric and Heteromeric Kinesins
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Review: regulation mechanisms of Kinesin-1
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Unique Post-Translational Modifications in Specialized Microtubule Architecture
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The reciprocal coordination and mechanics of molecular motors in living cells
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Heterodimerization of the Two Motor Subunits of the Heterotrimeric Kinesin, KRP85/95
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The Processivity of Kinesin-2 Motors Suggests Diminished Front-Head Gating
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Cho, K., Yi, H., Desai, R. M., Hand, A. R., Haas, A. L., & Ferreira, P. A. (2009) · EMBO Reports · doi:10.1038/embor.2009.29 · Cited by 58 · see citing works
An isoform of kinesin light chain specific for the Golgi complex
Gyoeva, F. K., Bybikova, E. M., & Minin, A. А. (2000) · Journal of Cell Science · doi:10.1242/jcs.113.11.2047 · Cited by 57 · see citing works
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Half-Site Inhibition of Dimeric Kinesin Head Domains by Monomeric Tail Domains
Hackney, D. D., Baek, N., & Snyder, A. C. (2009) · Biochemistry · doi:10.1021/bi8022575 · Cited by 54 · see citing works
Drosophila PAT1 is required for Kinesin-1 to transport cargo and to maximize its motility
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Kinesin velocity increases with the number of motors pulling against viscoelastic drag
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Intracellular imaging of targeted proteins labeled with quantum dots
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Kinesin’s light chains inhibit the head- and microtubule-binding activity of its tail
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Force–Velocity Curves of Motor Proteins Cooperating In Vivo
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Analysis of heterodimer formation by Xklp3A/B, a newly cloned kinesin‐II from Xenopus laevis
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KAP, the Accessory Subunit of Kinesin-2, Binds the Predicted Coiled-Coil Stalk of the Motor Subunits
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The Tetrameric Molecule of Conventional Kinesin Contains Identical Light Chains
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Mechanism of cooperative behaviour in systems of slow and fast molecular motors
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Chana, M., Tripet, B., Mant, C., & Hodges, R. (2008) · Journal of Peptide Research · doi:10.1111/j.1399-3011.2005.00210.x · Cited by 29 · see citing works
The Kinesin-1 Tail Conformationally Restricts the Nucleotide Pocket
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Kinetic and Mechanistic Basis of the Nonprocessive Kinesin-3 Motor NcKin3
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Flexibility of the Neck Domain Enhances Kinesin-1 Motility under Load
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Fractionation and Characterization of Kinesin II Species in Vertebrate Brain
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Torque generation by one of the motor subunits of heterotrimeric kinesin-2
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Bidirectional Transport: Matchmaking for Motors
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Dimerization properties of a Xenopus laevis kinesin‐II carboxy‐terminal stalk fragment
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Kinesin passing permanent blockages along its protofilament track
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Single Molecular Observation of Self-Regulated Kinesin Motility
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Dissection of Kinesin's Processivity
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Properties of the Kinesin‐3 NcKin3 motor domain and implications for neck function
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Variational approach to molecular kinetics
Nüske, F., Keller, B. G., Pérez-Hernández, G., Mey, A. S. J. S., & Noé, F. (2014) · Journal of Chemical Theory and Computation · doi:10.1021/ct4009156 · Cited by 308 · see citing works
Melanocytes in the Skin – Comparative Whole Transcriptome Analysis of Main Skin Cell Types
Reemann, P., Reimann, E., Ilmjärv, S., Porosaar, O., Silm, H., Jaks, V., Vasar, E., Kingo, K., & Kõks, S. (2014) · PLoS ONE · doi:10.1371/journal.pone.0115717 · Cited by 64 · see citing works
Regulation of ciliary membrane protein trafficking and signalling by kinesin motor proteins
Morthorst, S. K., Christensen, S. T., & Pedersen, L. B. (2018) · The FEBS Journal · doi:10.1111/febs.14583 · Cited by 49 · see citing works
Chiarelli, N., Carini, G., Zoppi, N., Ritelli, M., & Colombi, M. (2018) · PLOS ONE · doi:10.1371/journal.pone.0191220 · Cited by 45 · see citing works
Woll, K. A., Guzik-Lendrum, S., Bensel, B. M., Bhanu, N. V., Dailey, W. P., Garcia, B. A., Gilbert, S. P., & Eckenhoff, R. G. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.002182 · Cited by 23 · see citing works
- Authors
- Verhey, K. J., Kaul, N., & Soppina, V.
- Affiliations
- University of Michigan (US)
- Venue
- Annual Review of Biophysics
- Publisher
- Annual Reviews
- Published
- 2011-06-09
- Volume
- 40
- Issue
- 1
- Pages
- 267-288
- ISSN
- 1936-122X (ISSN-L)
- 1936-1238
- OpenAlex
- W2124852145
- Semantic Scholar
- 21a1ae44a7ade38d091ac9effab6cca3e82c3508
- Cited by
- 231
- References
- 155
- Citations by year
- 2026: 10 · 2025: 10 · 2024: 9 · 2023: 12 · 2022: 29 · 2021: 21 · 2020: 17 · 2019: 15 · 2018: 20 · 2017: 8 · 2016: 10 · 2015: 14 · 2014: 16 · 2013: 14 · 2012: 19
- FWCI
- 1.48
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Annual Review of Biophysics (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Institute of General Medical Sciences (R01GM070862)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Keywords
- kinesin, kinesin motor domain, kinesin-1, kinesin-2, kinesin-3, kinesin superfamily, intracellular transport, microtubule motor proteins, cargo binding, force generation, in vitro to in vivo translation
- MeSH terms
- Binding Sites, Cell Movement, Computer Simulation, Models, Biological, Models, Chemical, Protein Binding, Kinesins, Molecular Motor Proteins
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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