Cited by 131Microtubule and mitosis dynamicsProtein Structure and DynamicsAdvanced Fluorescence Microscopy Techniques

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Conformational changes during kinesin motility

Schief, William R, Howard, Jonathon·2001·Current Opinion in Cell Biology

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Abstract

Nucleotide-dependent movements of the head and neck of kinesin have been visualized by cryoelectron microscopy and have been inferred from single-molecule studies. Key predictions of the hand-over-hand model for dimeric kinesin have been confirmed, and a novel processivity mechanism for the one-headed, kinesin-related motor KIF1A has been discovered.

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Theoclitou, M., Aquila, B. M., Block, M. H., Brassil, P. J., Castriotta, L., Code, E. L., Collins, M. P., Davies, A. M., Deegan, T. L., Jayachandran, E., et al. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm200629m · Cited by 48
Small Crowders Slow Down Kinesin-1 Stepping by Hindering Motor Domain Diffusion
Sozański, K., Ruhnow, F., Wiśniewska, A., Tabaka, M., Diez, S., & Hołyst, R. (2015) · Physical Review Letters · doi:10.1103/physrevlett.115.218102 · Cited by 43
Monte Carlo Analysis of Neck Linker Extension in Kinesin Molecular Motors
Kutys, M. L., Fricks, J., & Hancock, W. O. (2010) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1000980 · Cited by 37
“This model is built on a large body of kinesin biophysical and biochemical studies [3,4,6,15,16] and was recently used to investigate differences between Kinesin-1 and Kinesin-2 motors [17,18].”
Background
The Tumbleweed: Towards a synthetic protein motor
Bromley, E. H. C., Kuwada, N. J., Zuckermann, M. J., Donadini, R., Samii, L., Blab, G. A., Gemmen, G. J., Lopez, B. J., Curmi, P. M. G., Forde, N. R., et al. (2009) · HFSP journal · doi:10.2976/1.3111282 · Cited by 41
“For example, the motor domain of kinesin has subtly different conformations in up to five different liganddependent states (involving three different possible nucleotide bound states and two track binding states) (Schief and Howard, 2001).”
Background
Mechanics of motor proteins
Howard, J. (2007) · Springer eBooks · doi:10.1007/3-540-45701-1_2 · Cited by 29
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Kinesin Motor Enzymology: Chemistry, Structure, and Physics of Nanoscale Molecular Machines
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EPR spectroscopy shows a microtubule-dependent conformational change in the kinesin switch 1 domain.
Naber, N., Rice, S., Matuska, M., Vale, R., Cooke, R., & Pate, E. (2003) · Biophysical Journal · doi:10.1016/s0006-3495(03)70043-5 · Cited by 31
“…changes in both myosin and the G-proteins, a popular hypothesis is that this latter coordination is an essential element for motility (Vale and Milligan, 2000; Smith and Rayment, 1996; Kull and Endow, 2002; Woehlke, 2001; Holmes and Geeves, 2000; Cooke, 1997; Schief and Howard, 2001).”
Background
Motor Proteins as Nanomachines: The Roles of Thermal Fluctuations in Generating Force and Motion
Howard, J. (2010) · Springer eBooks · doi:10.1007/978-3-0346-0428-4_3 · Cited by 23
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Flexibility of the Neck Domain Enhances Kinesin-1 Motility under Load
Jaud, J., Bathe, F., Schliwa, M., Rief, M., & Woehlke, G. (2006) · Biophysical Journal · doi:10.1529/biophysj.105.076265 · Cited by 28
Parsing the roles of neck-linker docking and tethered head diffusion in the stepping dynamics of kinesin
Zhang, Z., Goldtzvik, Y., & Thirumalai, D. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1706014114 · Cited by 30
Cellular Motors for Molecular Manufacturing
Dinu, C. Z., Chrisey, D. B., Diez, S., & Howard, J. (2007) · The Anatomical Record · doi:10.1002/ar.20599 · Cited by 22
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Single molecule processes on the stepwise movement of ATP-driven molecular motors
Nishiyama, M., Higuchi, H., Ishii, Y., Taniguchi, Y., & Yanagida, T. (2003) · Biosystems · doi:10.1016/s0303-2647(03)00122-9 · Cited by 30
Helix Capping Interactions Stabilize the N-Terminus of the Kinesin Neck Coiled-Coil
Tripet, B., & Hodges, R. S. (2002) · Journal of Structural Biology · doi:10.1006/jsbi.2002.4475 · Cited by 24
“Continuation of these movements results in continuous processive movement of the kinesin molecule along the microtubule filament (Vale and Milligan, 2000; Schief and Howard, 2001).”
Background
Insight into the chemomechanical coupling mechanism of kinesin molecular motors
Xie, P. (2021) · Communications in Theoretical Physics · doi:10.1088/1572-9494/abecd8 · Cited by 30
“…the forward stepping of the motor is driven mainly by a large conformational change of the NL ( termed as NL docking ) induced by ATP binding [ 27 – 31 ] , namely the forward stepping is mainly via the power-stroke ( PS ) mechanism, and thus this class is called NL-docking model ( or PS model )…”
Kinesins with Extended Neck Linkers: A Chemomechanical Model for Variable-Length Stepping
Hughes, J., Hancock, W. O., & Fricks, J. (2011) · Bulletin of Mathematical Biology · doi:10.1007/s11538-011-9697-6 · Cited by 20
“4.1 Purely Chemical Model A common motor model assumes that a motor must pass through a sequence of chemical states in order to take a step (Hancock and Kinesin 2003; Block 2007; Vale and Milligan 2000; Schief and Howard 2001; Cross 2004).”
Influential
Monte Carlo study of substrate-induced folding and refolding of lattice proteins.
Coluzza, I., & Frenkel, D. (2007) · Biophysical Journal · doi:10.1529/biophysj.106.084236 · Cited by 23
“Motor proteins (1–3) are an example of this class of proteins.”
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Frey, E., & Vilfan, A. (2002) · Chemical Physics · doi:10.1016/s0301-0104(02)00553-0 · Cited by 34
Microtubule−Kinesin Interface Mutants Reveal a Site Critical for Communication
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“Kinesin uses the energy of ATP hydrolysis to generate unidirectional processive movement along microtubules (1-4).”
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A matrix computational approach to kinesin neck linker extension
Hughes, J., Hancock, W. O., & Fricks, J. (2010) · Journal of Theoretical Biology · doi:10.1016/j.jtbi.2010.10.005 · Cited by 18
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Reverse Engineering: Learning from Proteins How to Enhance the Performance of Synthetic Nanosystems
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Fluctuations and randomness of movement of the bead powered by a single kinesin molecule in a force-clamped motility assay: Monte Carlo simulations.
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“It is generally believed that the mechanical translocation of kinesins on an MT proceeds by a handover-hand mechanism (Cross, 1995; Gelles et al., 1995; Peskin and Oster, 1995; Romberg et al., 1998; Hancock and Howard, 1999; Schief and Howard, 2001), in which one head is always attached to the MT while the other head…”
Background
Heat‐shock protein 70 binds microtubules and interacts with kinesin in tobacco pollen tubes
Parrotta, L., Cresti, M., & Cai, G. (2013) · Cytoskeleton · doi:10.1002/cm.21134 · Cited by 14
“Consequently, the conformational change induced by AMPPNP in the kinesin molecule, by increasing its affinity for microtubules [Schief and Howard, 2001], might be required to facilitate the binding of HSP70.”
Background
Creatine Kinase Equilibration and ΔGATP over an Extended Range of Physiological Conditions: Implications for Cellular Energetics, Signaling, and Muscle Performance
Wiseman, R. W., Brown, C. M., Beck, T. W., Brault, J. J., Reinoso, T. R., Shi, Y., & Chase, P. B. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241713244 · Cited by 14
“The dependence of actomyosin function on ∆GATP is mechanistically important for understanding the energetics of actomyosin’s ATPase cycle and for assessing physiological changes during hypoxia and muscle fatigue, where there are substantial alterations in cytosolic metabolite concentrations and cellular energy status.”
BackgroundInfluential
Long-range electrostatic interactions significantly modulate the affinity of dynein for microtubules
Pabbathi, A., Coleman, L. B., Godar, S. C., Paul, A., Garlapati, A., Spencer, M., Eller, J., & Alper, J. (2022) · Biophysical Journal · doi:10.1016/j.bpj.2022.03.029 · Cited by 11
Renewal processes and fluctuation analysis of molecular motor stepping
Santos, J. E., Franosch, T., Parmeggiani, A., & Frey, E. (2005) · Physical Biology · doi:10.1088/1478-3975/2/3/008 · Cited by 10
“Linear processive motor proteins, of which myosin V and kinesin [3, 4] are important examples,”
BackgroundMethod
Directionality of kinesin motors.
Kasprzak, A. A., & Hajdo, Ł. (2002) · Acta Biochimica Polonica · doi:10.18388/abp.2002_3741 · Cited by 9
A common chemomechanical coupling model for orphan and conventional kinesin molecular motors
Guo, S., & Xie, P. (2020) · Biophysical Chemistry · doi:10.1016/j.bpc.2020.106427 · Cited by 10
Renewal-Reward Process Formulation of Motor Protein Dynamics
Krishnan, A., & Epureanu, B. I. (2011) · Bulletin of Mathematical Biology · doi:10.1007/s11538-011-9632-x · Cited by 10
“Some studies focus on characterizing structural aspects like the different conformations of the protein and how these help it function (Geeves and Holmes 1999 ;R ice et al.1999; Schief and Howard 2001 ).”
BackgroundInfluential
Neck-Linker-Length Dependence of Processive Kinesin-5 Motility
Düselder, A., Thiede, C., Kramer, S., Schmidt, C., & Lakämper, S. (2011) · doi:10.1016/j.bpj.2010.12.876 · Cited by 8
Effect of the Neck Linker on Processive Stepping of Kinesin Motor
Xie, P. (2023) · Biophysica · doi:10.3390/biophysica3010004 · Cited by 11
Effect of the number of molecules on the energetic efficiency in molecular motors using the Flashing Ratchet model
Mouri, K., & Shimokawa, T. (2008) · Physica A Statistical Mechanics and its Applications · doi:10.1016/j.physa.2008.05.017 · Cited by 9
Harnessing microtubule dynamic instability for nanostructure assembly
Bouchard, A. M., Warrender, C., & Osbourn, G. C. (2006) · Physical Review E · doi:10.1103/physreve.74.041902 · Cited by 6
Mechanism of Processive Movement of Monomeric and Dimeric Kinesin Molecules
Xie, P. (2010) · International Journal of Biological Sciences · doi:10.7150/ijbs.6.665 · Cited by 47
Glu415 in the α-tubulins plays a key role in stabilizing the microtubule–ADP-kinesin complexes
Gáspár, I., & Szabad, J. (2009) · Journal of Cell Science · doi:10.1242/jcs.050252 · Cited by 6
“from ATP to mechanical force exertion (Schief and Howard, 2001).”
Background
Kinesin–ADP: whole lotta shakin' goin' on
Quinlan, M., Forkey, J., & Goldman, Y. (2001) · Nature Structural Biology · doi:10.1038/88522 · Cited by 6
Plus and minus ends of microtubules respond asymmetrically to kinesin binding by a long-range directionally driven allosteric mechanismPreprint
Vu, H. T., Zhang, Z.-C., Tehver, R., & Thirumalai, D. (2021) · bioRxiv · doi:10.1101/2021.08.30.458176 · Cited by 5
“Next, we analyzed the changes in the MT dynamics induced by a Kin1 monomer, which is of particular interest because for processive motion, one of the heads has to be bound to the MT at all times [1, 2, 25, 26, 27, 28, 29].”
Background
Molecular Motors: Single-Molecule Recordings Made Easy
Diez, S., Schief, W. R., & Howard, J. (2002) · Current Biology · doi:10.1016/s0960-9822(02)00750-9 · Cited by 3
“The debate in the field has been whether the rear head detaches in the K·ADP or the K·ADP·Pi state [17], but unfortunately Yajima et al.”
BackgroundSelf-citation
4.17 Kinesin Structure and Biochemistry
Gilbert, S. P., & Sardar, H. (2012) · Elsevier eBooks · doi:10.1016/b978-0-12-374920-8.00421-5 · Cited by 6
Analysis of biological motors via multidimensional fractionation: A strategy
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Master Equation Approach to Molecular Motor’s Directed Motion
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Synthesis of N-(1-(6-acetamido-5-phenylpyrimidin-4-yl) piperidin-3-yl) amide derivatives as potential inhibitors for mitotic kinesin spindle protein
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A simulation model of the conventional kinesin based on the Driven-by-Detachment mechanism
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A Model for Chemomechanical Coupling of Kinesin-3 Motor
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A mechanical model for the role of the neck linker during kinesin stepping and gating
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Flexibility of the neck-linker during docking is pivotal for function of bi-directional kinesin
Goldstein-Levitin, A., Allhuzaeel, K., Pandey, H., & Gheber, L. (2020) · bioRxiv · doi:10.1101/2020.05.27.118430

Authors: Schief, W. R., & Howard, J.
Affiliations: University of Washington (US)
Corresponding author: Schief, William R
Howard, Jonathon
ORCID: Schief, William R
Howard, Jonathon
Venue: Current Opinion in Cell Biology
Publisher: Elsevier BV
Published: 2001-02
Volume: 13
Issue: 1
Pages: 19-28
ISSN: 0955-0674 (ISSN-L)
DOI: 10.1016/s0955-0674(00)00169-1
OpenAlex: W2170893640
Cited by: 131
References: 0
Citations by year: 2025: 1 · 2024: 1 · 2023: 3 · 2022: 3 · 2021: 3 · 2020: 1 · 2018: 2 · 2017: 1 · 2016: 1 · 2015: 5 · 2014: 2 · 2013: 4 · 2012: 5
FWCI: 1.19
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Current Opinion in Cell Biology (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biophysics › Advanced Fluorescence Microscopy Techniques
Keywords: kinesin, conformational change, KIF1A, motor processivity, single-molecule analysis, cryo-electron microscopy
MeSH terms: Animals, Models, Molecular, Protein Conformation, Kinesins, Molecular Motor Proteins

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Conformational changes during kinesin motility

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