Conformational changes during kinesin motility
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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Allosteric communication between the two kinesin motor domains is mediated through the internal load generated when both heads attach to the microtubule.
“Several lines of evidence suggest that this allosteric communication is mediated through the internal load generated when both heads attach to the microtubule”
From Stepping and Stretching (2003) · cites this paper as [13]
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“Although evidence for this conformational change has been obtained (Rosenfeld et al., 2001; Skiniotis et al., 2003; Tomishige et al., 2006), it still remains controversial whether the neck linker docking powers kinesin movement (Schief and Howard, 2001; Block, 2007; Carter and Cross, 2005).”
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“The detailed mechanism of motion is subject of ongoing research (Schief & Howard, 2001).”
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“However, the neck linker conformational state model has been questioned in kinesin dimers, and alternative models for kinesin processivity have been suggeste”
BackgroundInhibition of kinesin motility by ADP and phosphate supports a hand-over-hand mechanism
Schief, W. R., Clark, R. H., Crevenna, A. H., & Howard, J. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0304369101 · Cited by 119 · see citing works
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“In the full, two-headed motor, the position of the neck-linker and its relationship to the particular nucleotide in the active site may be different from what is found in one-headed constructs [16].”
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“In studies of other processive motors, such as myosin V (reviewed in [51]) and conventional kinesin (reviewed in [52]), a mechanism has been proposed in which two identical motor domains alternatively swing forward at each step while one motor domain remains attached on the track.”
BackgroundKlumpp, L. M., Hoenger, A., & Gilbert, S. P. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0307691101 · Cited by 107 · see citing works
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Elastic lever-arm model for myosin V.
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“An approach that has been applied to myosin V (Kolomeisky and Fisher, 2003), kinesin (Peskin and Oster, 1995; Schief and Howard, 2001; Thomas et al., 2002), as well as to other biological mechanisms of force generation, including actin polymerization (Peskin et al.”
BackgroundMethodWhat kinesin does at roadblocks: the coordination mechanism for molecular walking
Crevel, I. M., Nyitrai, M., Alonso, M. C., Weiss, S., Geeves, M. A., & Cross, R. A. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600042 · Cited by 88 · see citing works
“Howard and colleagues (Schief and Howard, 2001) have argued, based on the measured behaviour of a one-headed kinesin dimer, that the ATP-induced detachment of trail heads in intact dimers must be o1 s (1), requiring therefore a processivity scheme with substantial acceleration of trail head detachment by lead head att…”
BackgroundDirect Long-Term Observation of Kinesin Processivity at Low Load
Yajima, J., Alonso, M. C., Cross, R. A., & Toyoshima, Y. Y. (2002) · Current Biology · doi:10.1016/s0960-9822(01)00683-2 · Cited by 80 · see citing works
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“This observation suggests that in the absence of ATP (as in the NN state) one of the two motor domains is prevented from interacting with the microtubul”
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“…at the N-terminus of the fulllength kinesin protein, this is often cited to be the necklinker (Kull and Endow, 2002; Mather and Fox, 2006; Rice et al., 1999; Schief and Howard, 2001), but recent experiments instead point this role to the kinesin cover neck (Hwang et al., 2008; Khalil et al., 2008).”
BackgroundInfluentialKIF1D is a fast non‐processive kinesin that demonstrates novel K‐loop‐dependent mechanochemistry
Rogers, K. R., Weiss, S., Crevel, I., Brophy, P. J., Geeves, M., & Cross, R. (2001) · The EMBO Journal · doi:10.1093/emboj/20.18.5101 · Cited by 73 · see citing works
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BackgroundReview: regulation mechanisms of Kinesin-1
Adio, S., RETH, J., Bathe, F., & Woehlke, G. (2006) · Journal of Muscle Research and Cell Motility · doi:10.1007/s10974-005-9054-1 · Cited by 66 · see citing works
“However, other explanations are also possible (Schief and Howard, 2001).”
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“Both run length and velocity distributions are significantly different (FL), 125 (1–657), 76 (657–1624) particles; n = 90 MTs/condition. from MT pelleting assay; 5 mM MTs, 10 mM AMPPNP. say; 5 mM MTs, 10 mM AMPPNP; MTs in right lanes digested with 200 mg/mL Neuron 92, 1–16, November 23, 2016 5 Figure 3.”
InfluentialBiomimetic actuators: where technology and cell biology merge
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Key residues on microtubule responsible for activation of kinesin ATPase
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“Force generation is coupled to the entire process of state transition (Figure 6B–D), from the diffusional binding state to the strong-binding, nucleotide-free state (Schief and Howard, 2001; Cross, 2004).”
BackgroundClosing of the Nucleotide Pocket of Kinesin-Family Motors upon Binding to Microtubules
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“One model involves a hand-over-hand stepping mechanism in which the two heads of the motor alternate in binding to the microtubule and hydrolyzing ATP, each head in turn taking a step to advance the motor towards the microtubule plus end (Howard, 2001; Schief and Howard, 2001).”
BackgroundKinesin’s backsteps under mechanical load
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Two Distinct Modes of Processive Kinesin Movement in Mixtures of ATP and AMP-PNP
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Ovechkina, Y., & Wordeman, L. (2003) · Traffic : the International Journal of Intracellular Transport · doi:10.1034/j.1600-0854.2003.00099.x · Cited by 48 · see citing works
“All conventional kinesins (Kin N subfamily members) characterized so far are processive, meaning they are able to take hundreds of steps before dissociating from an MT filament [reviewed in (14,15)].”
BackgroundCoordination of kinesin's two heads studied with mutant heterodimers
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“Although the contribution of the neck linker docking is well established, there are still some arguments regarding whether this docking powers kinesin movement (Nishiyama et al, 2001, 2002; Schief and Howard, 2001; Carter and Cross, 2005; Block, 2007).”
Kinesin motors as molecular machines.
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“The stepping mechanism of conventional kinesin is currently controversial: most workers favor a hand-over-hand mechanism in which the two heads of the motor bind alternatively to the microtubule and hydrolyze ATP.((30,46)) However, some researchers have proposed amodel in which only one of the twoheads hydrolyzesATPan…”
BackgroundSingle Fungal Kinesin Motor Molecules Move Processively along Microtubules
Lakämper, S., Kallipolitou, A., Woehlke, G., Schliwa, M., & Meyhöfer, E. (2003) · Biophysical Journal · doi:10.1016/s0006-3495(03)74991-1 · Cited by 44 · see citing works
Kinesin's step dissected with single-motor FRET
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Small Crowders Slow Down Kinesin-1 Stepping by Hindering Motor Domain Diffusion
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Monte Carlo Analysis of Neck Linker Extension in Kinesin Molecular Motors
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“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].”
BackgroundThe 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 · see citing works
“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).”
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Self-citationKinesin 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 · see citing works
“…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).”
BackgroundMotor 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 · see citing works
Self-citationFlexibility 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 · see citing works
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Cellular Motors for Molecular Manufacturing
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Self-citationSingle 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 · see citing works
Helix capping interactions stabilize the N-terminus of the kinesin neck coiled-coil.
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“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).”
BackgroundInsight 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 · see citing works
“…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., & Fricks, J. (2011) · Bulletin of Mathematical Biology · doi:10.1007/s11538-011-9697-6 · Cited by 23 · see citing works
“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).”
InfluentialMonte 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 · see citing works
“Motor proteins (1–3) are an example of this class of proteins.”
Anomalous relaxation kinetics of biological lattice–ligand binding models
Frey, E., & Vilfan, A. (2002) · Chemical Physics · doi:10.1016/s0301-0104(02)00553-0 · Cited by 23 · see citing works
Microtubule−Kinesin Interface Mutants Reveal a Site Critical for Communication
Klumpp, L. M., Brendza, K. M., Gatial, J. E., Hoenger, A., Saxton, W. M., & Gilbert, S. P. (2004) · Biochemistry · doi:10.1021/bi035830e · Cited by 20 · see citing works
“Kinesin uses the energy of ATP hydrolysis to generate unidirectional processive movement along microtubules (1-4).”
BackgroundMethodA matrix computational approach to kinesin neck linker extension.
Hughes, J., Hancock, W., & Fricks, J. (2011) · Journal of Theoretical Biology · doi:10.1016/j.jtbi.2010.10.005 · Cited by 19 · see citing works
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Reverse Engineering: Learning from Proteins How to Enhance the Performance of Synthetic Nanosystems
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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…”
BackgroundHeat‐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.”
BackgroundWiseman, 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 · see citing works
“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.”
BackgroundInfluentialLong-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 · see citing works
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 · see citing works
“Linear processive motor proteins, of which myosin V and kinesin [3, 4] are important examples,”
BackgroundMethodDirectionality of kinesin motors.
Kasprzak, A. A., & Hajdo, Ł. (2002) · Acta Biochimica Polonica · doi:10.18388/abp.2002_3741 · Cited by 9 · see citing works
A common chemomechanical coupling model for orphan and conventional kinesin molecular motors.
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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 · see citing works
“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 ).”
BackgroundInfluentialNeck-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
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Harnessing microtubule dynamic instability for nanostructure assembly.
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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 46 · see citing works
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 · see citing works
“from ATP to mechanical force exertion (Schief and Howard, 2001).”
BackgroundKinesin–ADP: whole lotta shakin' goin' on
Quinlan, M., Forkey, J., & Goldman, Y. (2001) · Nature Structural Biology · doi:10.1038/88522 · Cited by 6 · see citing works
Vu, H. T., Zhang, Z.-C., Tehver, R., & Thirumalai, D. (2021) · bioRxiv · doi:10.1101/2021.08.30.458176 · Cited by 5 · see citing works
“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].”
BackgroundMolecular motors: single-molecule recordings made easy.
Diez, S., Schief, W., & Howard, J. (2002) · Current Biology · doi:10.1016/s0960-9822(02)00750-9 · Cited by 5 · see citing works
“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-citation4.17 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 · see citing works
Analysis of biological motors via multidimensional fractionation: A strategy
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Micromechanics of Molecular Motors: Experiments and Theory
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Goldstein-Levitin, A., Pandey, H., Allhuzaeel, K., Kass, I., & Gheber, L. (2021) · eLife · doi:10.7554/elife.71036 · Cited by 3 · see citing works
Master Equation Approach to Molecular Motor’s Directed Motion
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Nucleotide-dependent structural fluctuations and regulation of microtubule-binding affinity of KIF1A
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A simulation model of the conventional kinesin based on the Driven-by-Detachment mechanism
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“While processively moving, a kinesin dimer hydrolyzes one ATP molecule per each 8-nm step (Hua et al., 1997; Schnitzer and Block, 1997).”
BackgroundA Model for Chemomechanical Coupling of Kinesin-3 Motor
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In vivo collection of rare proteins using kinesin-based "nano-harvesters".
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Analysis of kinesin mechanochemistry via simulated annealingPreprint
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“(a) From (24), (b) From (18), (c) From (15), and (d) From (25).”
BackgroundMethodInfluentialA mechanical model for the role of the neck linker during kinesin stepping and gating
Wang, H., & He, C. (2011) · Science China Physics Mechanics and Astronomy · doi:10.1007/s11433-011-4509-4 · Cited by 1 · see citing works
How Is a Protein Molecule Nearsighted
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Effective Potential of a Two-State Model for Molecular Motor
Han, Y.-R., Zhao, T.-J., & Yan, W.-L. (2005) · doi:10.1088/0253-6102/43/2/035 · Cited by 1
Mechanical-to-Chemical Transduction by Motor Proteins
Howard, J. (2003) · doi:10.1142/9789812704931_0004 · Cited by 1
Self-citationA multiscale modeling approach for biomolecular systems
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Rotation-translation coupling of a double-headed Brownian motor in a traveling-wave potential
Wu, W.-X., Li, C.-P., Song, Y.-L., Han, Y., & Zheng, Z.-G. (2021) · Frontiers of Physics · doi:10.1007/s11467-021-1057-x
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
- Venue
- Current Opinion in Cell Biology
- Publisher
- Elsevier BV
- Published
- 2001-02
- Volume
- 13
- Issue
- 1
- Pages
- 19-28
- ISSN
- 0955-0674 (ISSN-L)
- 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
- 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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