Kinetic Mechanism of a Monomeric Kinesin Construct
Open accessAbstract
The kinetic mechanism is analyzed for a monomeric human kinesin construct K332. In the absence of microtubules, the rate constants of the ATPase cycle are very similar to dimeric human kinesin K379 and whole kinesin from bovine brain. The microtubule-activated ATPase is 60 s(-1) at 20 degrees C; Km(Mt) is 5 microM; dissociation constants in the presence of ATP and ADP are 9 microM and 16 microM, respectively. The values of dissociation constants are 5 times larger than for K379. Binding of K332 to microtubules increased the rate of the hydrolysis step from 7 s(-1) to greater than 200 s(-1) and the 2'-(3')-O-(N-methylanthraniloyl) (mant) ADP dissociation step from 0.02 s(-1) to greater than 100 s(-1). At higher ionic strength, more than one ATP is hydrolyzed before dissociation of MtK332 (small processivity). Data are fitted to the kinetic scheme. [equation: see text] Approximate values of rate constants are k1 = 500 s(-1), k2 > or = 200 s(-1), k3k4/(k3 + k4) = 100 s(-1), k(dis) = 80+/-10 s(-1). Two experiments to measure k4 gave 110 s(-1) from the maximum rate of dissociation of mant ADP for reaction of K x ADP with microtubules and 300 s(-1) from extrapolation to zero concentration of rate of binding of mant ADP to MtK. It is proposed that mant ADP dissociation is a two-step process. In the simple scheme, k4 is the effective rate of the two-step release of ADP, k4 = 150 s(-1) to 200 s(-1), and k3 = 150 s(-1) to 200 s(-1) to account for the steady state rate.
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Direct measurements show that kh is ∼100 s−1 for dimeric constructs and considerably faster for monomers, with estimates placing it at >250 s−1.
“Direct measurements using chemical quench methods have consistently shown that, althoughkh is ∼100 s−1 for dimeric constructs, it is considerably faster for monomers, with estimates placing it at >250 s−1 (2”
From Stepping and Stretching (2003) · cites this paper as [2]
In “The Hydrolysis Step” (page not supplied), the monomer’s phosphate-burst transient is reported as >250 s−1, but the paper estimates the hydrolysis step itself at ≥200 s−1—not >250 s−1. The cited passages also do not establish a hydrolysis rate of approximately 100 s−1 for dimeric constructs. (LLM, conf=0.90)
Experimental — accuracy not yet measuredMembers of the kinesin family of molecular motors are capable of taking over 100 steps on their microtubule track without dissociating.
“Members of the kinesin family of molecular motors are capable of taking over 100 steps on their microtubule track without dissociating”
From Stepping and Stretching (2003) · cites this paper as [2]
The Abstract and Pathway of Dissociation section describe a monomeric kinesin construct with small processivity: it can complete more than one ATPase cycle before dissociating. The paper does not establish that kinesin motors take over 100 steps along a microtubule without dissociating. (LLM, conf=0.82)
Experimental — accuracy not yet measured
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Cites
Fisher, A. J., Smith, C. A., Thoden, J. B., Smith, R., Sutoh, K., Holden, H. M., & Rayment, I. (1995) · Biochemistry · doi:10.1021/bi00028a004 · Cited by 593 · see citing works
Smith, C. A., & Rayment, I. (1996) · Biochemistry · doi:10.1021/bi952633+ · Cited by 487 · see citing works
Evidence for alternating head catalysis by kinesin during microtubule-stimulated ATP hydrolysis.
Hackney, D. D. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.15.6865 · Cited by 351 · see citing works
Pathway of processive ATP hydrolysis by kinesin
Gilbert, S. P., Webb, M. R., Brune, M., & Johnson, K. A. (1995) · Nature · doi:10.1038/373671a0 · Cited by 250 · see citing works
Navone, F., Niclas, J., Hom-Booher, N., Sparks, L. L., Bernstein, H., McCaffrey, G., & Vale, R. D. (1992) · The Journal of Cell Biology · doi:10.1083/jcb.117.6.1263 · Cited by 194 · see citing works
Interacting Head Mechanism of Microtubule-Kinesin ATPase
Ma, Y.-Z., & Taylor, E. W. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.2.724 · Cited by 181 · see citing works
Self-citationWeak and strong states of kinesin and ncd.
Crevel, I., Lockhart, A., & Cross, R. A. (1996) · Journal of Molecular Biology · doi:10.1006/jmbi.1996.0147 · Cited by 155 · see citing works
Kinetic studies on the association and dissociation of myosin subfragment 1 and actin.
Taylor, E. W. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)52434-0 · Cited by 110
Self-citationMechanism of Microtubule Kinesin ATPase
Ma, Y. Z., & Taylor, E. W. (1995) · Biochemistry · doi:10.1021/bi00040a040 · Cited by 98 · see citing works
Self-citationShriver, J., & Sykes, B. (1981) · Biochemistry · doi:10.1021/bi00510a041 · Cited by 86
Huang, T., Suhan, J., & Hackney, D. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)31692-2 · Cited by 85
Pre-Steady-State Kinetics of the Microtubule.cntdot.Kinesin ATPase
Gilbert, S. P., & Johnson, K. A. (1994) · Biochemistry · doi:10.1021/bi00173a044 · Cited by 84 · see citing works
Kinetic mechanism of kinesin motor domain.
Ma, Y.-Z., & Taylor, E. W. (1995) · Biochemistry · doi:10.1021/bi00040a039 · Cited by 69 · see citing works
Self-citationA kinetic study of the kinesin ATPase.
Sadhu, A., & Taylor, E. W. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)49917-1 · Cited by 59 · see citing works
Self-citationEquilibrium studies of kinesin-nucleotide intermediates
Rosenfeld, S. S., Rener, B., Correia, J. J., Mayo, M. S., & Cheung, H. C. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.16.9473 · Cited by 56 · see citing works
Sedimentation studies on the kinesin motor domain constructs K401, K366, and K341
Correia, J. J., Gilbert, S. P., Moyer, M. L., & Johnson, K. A. (1995) · Biochemistry · doi:10.1021/bi00014a047 · Cited by 44 · see citing works
Subunit Interactions in Dimeric Kinesin Heavy Chain Derivatives That Lack the Kinesin Rod
Young, E. C., Berliner, E., Mahtani, H. K., Perez-Ramirez, B., & Gelles, J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.8.3926 · Cited by 42 · see citing works
Flagged first, then by citations
1 of the 18 references couldn’t be matched to a known paper.
Research works printed but not linked: 1
- Hackney, D. D. (1994) Proc. Natl. Acad. Sci. U. S. A. 91, 6865-6869
Cited by
Sorted by citations
Kinesin and dynein superfamily proteins in organelle transport and cell division
Hirokawa, N., Noda, Y., & Okada, Y. (1998) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(98)80087-2 · Cited by 364 · see citing works
The load dependence of kinesin’s mechanical cycle
Coppin, C. M., Pierce, D. W., Hsu, L., & Vale, R. D. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.16.8539 · Cited by 256 · see citing works
Hancock, W. O., & Howard, J. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.23.13147 · Cited by 243 · see citing works
The kinetic mechanism of kinesin.
Cross, R. (2004) · TIBS -Trends in Biochemical Sciences. Regular ed · doi:10.1016/j.tibs.2004.04.010 · Cited by 204 · see citing works
Rosenfeld, S. S., Fordyce, P. M., Jefferson, G. M., King, P. H., & Block, S. M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300849200 · Cited by 188 · see citing works
Interacting Head Mechanism of Microtubule-Kinesin ATPase
Ma, Y.-Z., & Taylor, E. W. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.2.724 · Cited by 181 · see citing works
Self-citationAn atomic-level mechanism for activation of the kinesin molecular motors
Sindelar, C., & Downing, K. (2010) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.0911208107 · Cited by 181 · see citing works
“Consequently, our models provide a qualitative explanation for why microtubules are required to fully stimulate catalysis (17): microtubule attachment is required to stabilize the switch II helix extension, so completing the array of stabilizing binding partners for the phosphate tube.”
Alternating Site Mechanism of the Kinesin ATPase
Gilbert, S. P., Moyer, M. L., & Johnson, K. A. (1998) · Biochemistry · doi:10.1021/bi971117b · Cited by 172 · see citing works
Structure of a kinesin–tubulin complex and implications for kinesin motility
Gigant, B., Wang, W., Dreier, B., Jiang, Q., Pecqueur, L., Plückthun, A., Wang, C.-G., & Knossow, M. (2013) · Nature Structural &Molecular Biology · doi:10.1038/nsmb.2624 · Cited by 167 · see citing works
A comparative proteomic analysis of tomato leaves in response to waterlogging stress.
Ahsan, N., Lee, D.-G., Lee, S.-H., Kang, K., Bahk, J., Choi, M., Lee, I.-J., Renaut, J., & Lee, B.-H. (2007) · Physiologia Plantarum : An International Journal for Plant Biology · doi:10.1111/j.1399-3054.2007.00980.x · Cited by 140
“ATP-binding/microtubulemotor contains a kinesin motor domain that possesses ATPase activity by which they convert chemical energy from ATP hydrolysis into mechanical forces that are essential for their motor activity (Ma and Taylor 1997).”
BackgroundThermodynamic properties of the kinesin neck-region docking to the catalytic core.
Rice, S. E., Cui, Y., Sindelar, C., Naber, N., Matuska, M., Vale, R., & Cooke, R. (2003) · Biophysical Journal · doi:10.1016/s0006-3495(03)74992-3 · Cited by 140 · see citing works
“5 A and have a significantly slowed release rate from the microtubule (Hancock and Howard, 1998; Jiang and Hackney, 1997; Ma and Taylor, 1997b; Moyer et al., 1998), indicating that detachment from the microtubule in the rear head may be accelerated by this strained conformation.”
BackgroundBacksteps induced by nucleotide analogs suggest the front head of kinesin is gated by strain
Guydosh, N. R., & Block, S. M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0600931103 · Cited by 132 · see citing works
Atherton, J., Farabella, I., Yu, I.-M., Rosenfeld, S., Houdusse, A., Topf, M., & Moores, C. (2014) · eLife · doi:10.7554/elife.03680.022 · Cited by 127
“600 Consistent with MT binding being important in the catalytic enhancement of 601 kinesins (Ma and Taylor, 1997), this hydrolysis competent configuration of the 602 switch loops is rarely seen in Mg-ATP-analogue kinesin structures in the 603 absence of MTs (e.”
BackgroundKikkawa, M., & Hirokawa, N. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601299 · Cited by 125 · see citing works
“In the absence of MTs, the NBP of kinesin is not fully open, since ADP release is slow (Hackney, 1988; Ma and Taylor, 1997).”
BackgroundKinetics of nucleotide-dependent structural transitions in the kinesin-1 hydrolysis cycle
Mickolajczyk, K. J., Deffenbaugh, N. C., Arroyo, J. O., Andrecka, J., Kukura, P., & Hancock, W. O. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1517638112 · Cited by 120 · see citing works
Inhibition 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
Conformational changes during kinesin motility
Schief, W. R., & Howard, J. (2001) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(00)00169-1 · Cited by 131 · see citing works
Loading direction regulates the affinity of ADP for kinesin
Uemura, S., & Ishiwata, S. (2003) · Nature Structural & Molecular Biology · doi:10.1038/nsb911 · Cited by 119 · see citing works
“The dissociation constant of ADP in the kinesin–microtubule complex in solution ( K , in the absence of external load) has been reported to be ∼50 μ”
BackgroundKinetic Characterization of a Monomeric Unconventional Myosin V Construct*
Trybus, K., Krementsova, E. B., & Freyzon, Y. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.39.27448 · Cited by 106 · see citing works
Mechanistic Analysis of the Mitotic Kinesin Eg5*
Cochran, J. C., Sontag, C., Maliga, Z., Kapoor, T. M., Correia, J., & Gilbert, S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404203200 · Cited by 98 · see citing works
[18] Fluorescent nucleotide analogs: Synthesis and applications
Jameson, D. M., & Eccleston, J. F. (1997) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(97)78020-0 · Cited by 111 · see citing works
To step or not to step? How biochemistry and mechanics influence processivity in Kinesin and Eg5
Valentine, M. T., & Gilbert, S. P. (2007) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2006.12.011 · Cited by 89 · see citing works
What 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
“Kinesin in the presence of the transition state analogues ADP.AlF4 and ADP.BeFx binds tightly to MT, suggesting that a transient K.ADP.Pi intermediate also binds tightly to MT (Crevel et al, 1996; Rosenfeld et al, 1996; Ma and Taylor, 1997b ).”
BackgroundInfluentialCochran, J. C., & Gilbert, S. (2005) · Biochemistry · doi:10.1021/bi051724w · Cited by 86 · see citing works
ATP Reorients the Neck Linker of Kinesin in Two Sequential Steps
Rosenfeld, S. S., Jefferson, G. M., & King, P. H. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103899200 · Cited by 84 · see citing works
Lethal Kinesin Mutations Reveal Amino Acids Important for ATPase Activation and Structural Coupling
Brendza, K. M., Rose, D. J., Gilbert, S. P., & Saxton, W. M. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.44.31506 · Cited by 85 · see citing works
Nucleotide‐induced conformations in the neck region of dimeric kinesin
Skiniotis, G., Surrey, T., Altmann, S., Gross, H., Song, Y.-H., Mandelkow, E., & Hoenger, A. (2003) · EMBO Journal · doi:10.1093/emboj/cdg164 · Cited by 79 · see citing works
A Chemically Reversible Brownian Motor: Application to Kinesin and Ncd
Astumian, R. D., & Derényi, I. (1999) · Biophysical Journal · doi:10.1016/s0006-3495(99)76950-x · Cited by 81 · see citing works
“We anticipate that transient experiments on the biochemical mechanisms of ATP hydrolysis by kinesin and ncd (Gilbert et al., 1995; Ma and Taylor, 1997; Pechatnikova and Taylor, 1997), can be used to further constrain the rate constants.”
BackgroundReview: Mechanochemistry of the kinesin‐1 ATPase
Cross, R. A. (2016) · Biopolymers · doi:10.1002/bip.22862 · Cited by 74 · see citing works
Docking and Rolling, a Model of How the Mitotic Motor Eg5 Works
Rosenfeld, S. S., Xing, J. W., Jefferson, G. M., & King, P. H. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m506561200 · Cited by 66 · see citing works
Kinetics: a tool to study molecular motors.
Gilbert, S., & Mackey, A. T. (2000) · Methods · doi:10.1006/meth.2000.1086 · Cited by 67 · see citing works
Hoeng, J., Dawson, S., House, S. A., Sagolla, M., Pham, J. K., Mancuso, J., Löwe, J., & Cande, W. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-11-1156 · Cited by 62 · see citing works
“It is known from previous work (Ma and Taylor, 1997) that in the absence of microtubules the release of ADP from the kinesin active site requires the stripping of the magnesium ion from the active site with EDTA or apyrase, whereby the magnesium exchange limits ADP exchange.”
BackgroundKey residues on microtubule responsible for activation of kinesin ATPase
Uchimura, S., Oguchi, Y., Hachikubo, Y., Ishiwata, S., & Muto, E. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.25 · Cited by 52 · see citing works
“Considering the reported result that MT binding accelerates the rate of ATP hydrolysis (Ma and Taylor, 1995, 1997), this step could also be disrupted in the a-E415A mutant.”
BackgroundClosing of the Nucleotide Pocket of Kinesin-Family Motors upon Binding to Microtubules
Naber, N., Minehardt, T. J., Rice, S., Chen, X.-R., Grammer, J., Matuska, M., Vale, R., Kollman, P., Car, R., Yount, R. G., et al. (2003) · Science · doi:10.1126/science.1082374 · Cited by 57 · see citing works
Motility of single one-headed kinesin molecules along microtubules.
Inoue, Y., Iwane, A., Miyai, T., Muto, E., & Yanagida, T. (2001) · Biophysical Journal · doi:10.1016/s0006-3495(01)75925-5 · Cited by 57 · see citing works
Kinetics processivity and the direction of motion of Ncd.
Pechatnikova, E., & Taylor, E. W. (1999) · Biophysical Journal · doi:10.1016/s0006-3495(99)76951-1 · Cited by 57 · see citing works
“In the case of kinesin, the rate of ADP dissociation is larger than the rate of dissociation of the kinesinzADP complex from the microtubule; consequently, monomeric kinesin exhibits kinetic processivity (Ma and Taylor, 1997a; Jiang and Hackney, 1997; Moyer et al., 1998).”
BackgroundInfluentialSelf-citationFoster, K. A., Correia, J. J., & Gilbert, S. P. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.52.35307 · Cited by 53 · see citing works
Measuring Kinesin's First Step
Rosenfeld, S. S., Xing, J., Jefferson, G. M., Cheung, H. C., & King, P. H. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m205261200 · Cited by 54 · see citing works
On the hand-over-hand mechanism of kinesin
Shao, Q., & Gao, Y. Q. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0602828103 · Cited by 48 · see citing works
A seesaw model for intermolecular gating in the kinesin motor protein
Sindelar, C. (2011) · Biophysical Reviews · doi:10.1007/s12551-011-0049-4 · Cited by 50 · see citing works
“In comparison, kinesin’s microtubule attachment affinity is 1 μM or lower in other observed nucleotide states (Rosenfeld et al. 1996; Ma and Taylor 1997).”
BackgroundPathway of ATP hydrolysis by monomeric kinesin Eg5.
Cochran, J. C., Krzysiak, T. C., & Gilbert, S. (2006) · Biochemistry · doi:10.1021/bi0608562 · Cited by 50 · see citing works
“A0 ) E0[k+2(k+2 + k-2)/(k+2 + k-2 + kslow) (2)] (5) FIGURE 1: Microtubule-activated steady-state ATPase of apoEg5.”
Two Distinct Modes of Processive Kinesin Movement in Mixtures of ATP and AMP-PNP
Subramanian, R., & Gelles, J. (2007) · The Journal of General Physiology · doi:10.1085/jgp.200709866 · Cited by 48 · see citing works
Insights into nucleotide binding in protein kinase A using fluorescent adenosine derivatives
Ni, D.-Q., Shaffer, J., & Adams, J. (2000) · Protein Science · doi:10.1110/ps.9.9.1818 · Cited by 48 · see citing works
“…derivatives of ATP have been used effectively for the study of molecular motors including myosin head fragments, dynein, and kinesin~e.g., Ma & Taylor, 1997; Friedman et al., 1998; Mocz et al., 1998; Moyer et al., 1998!, we wondered whether these derivatives would be useful for studying…”
Processivity of the Kinesin-2 KIF3A Results from Rear Head Gating and Not Front Head Gating
Chen, G.-Y., Arginteanu, D., & Hancock, W. O. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.628032 · Cited by 40 · see citing works
“This discrepancy was also observed for kinesin-1 (52), and the low affinity was supported by control experiments that measured the affinity of KIF3A for AMPPNP in solution to be nearly 2 orders of magnitude lower than the affinity for ADP (data not shown).”
BackgroundKinesin motility is driven by subdomain dynamics
Hwang, W., Lang, M. J., & Karplus, M. (2017) · eLife · doi:10.7554/elife.28948 · Cited by 43 · see citing works
Kinetic Mechanism of Monomeric Non-claret Disjunctional Protein (Ncd) ATPase*
Pechatnikova, E., & Taylor, E. W. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.49.30735 · Cited by 40 · see citing works
“The binding constant of MANT ADP to Ncd is probably 10 times larger than for K332, based on the ratio of rate constants of dissociation.”
BackgroundInfluentialSelf-citationThe structural kinetics of switch-1 and the neck linker explain the functions of kinesin-1 and Eg5
Muretta, J. M., Jun, Y., Gross, S. P., Major, J. A., Thomas, D. D., & Rosenfeld, S. S. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1512305112 · Cited by 37 · see citing works
Kinesin Has Three Nucleotide-dependent Conformations
Xing, J., Wriggers, W., Jefferson, G. M., Stein, R., Cheung, H. C., & Rosenfeld, S. S. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004232200 · Cited by 38 · see citing works
Li, M., & Zheng, W. (2011) · Biochemistry · doi:10.1021/bi2008257 · Cited by 41 · see citing works
Alternating Site ATPase Pathway of Rat Conventional Kinesin*
Auerbach, S., & Johnson, K. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m502984200 · Cited by 35 · see citing works
Pearson, D. S., Holtermann, G., Ellison, P., Cremo, C., & Geeves, M. (2002) · Biochemical Journal · doi:10.1042/bj20020462 · Cited by 35
“The simplest explanation of the results is that the two forms of mant-ADP are in competition for the nucleotide-binding pocket and have dierent anities for S1, as seen for kinesin [ 20 ,21].”
BackgroundMinehardt, T. J., Cooke, R., Pate, E., & Kollman, P. A. (2001) · Biophysical Journal · doi:10.1016/s0006-3495(01)76092-4 · Cited by 35 · see citing works
Interaction of the N‐terminal domain of MukB with the bacterial tubulin homologue FtsZ
Lockhart, A., & Kendrick-Jones, J. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)00677-2 · Cited by 32 · see citing works
Modeling Motility of the Kinesin Dimer from Molecular Properties of Individual Monomers†
Fan, D., Zheng, W., Hou, R., Li, F., & Wang, Z. (2008) · Biochemistry · doi:10.1021/bi800072p · Cited by 26 · see citing works
Bisaria, N., Greenfeld, M., Limouse, C., Pavlichin, D. S., Mabuchi, H., & Herschlag, D. (2016) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.1525082113 · Cited by 27
Characterization of a novel rice kinesin O12 with a calponin homology domain.
Umezu, N., Umeki, N., Mitsui, T., Kondo, K., & Maruta, S. (2011) · Journal of Biochemistry (Tokyo) · doi:10.1093/jb/mvq122 · Cited by 27 · see citing works
A conserved tyrosine in the neck of a fungal kinesin regulates the catalytic motor core
Schäfer, F., Deluca, D., Majdic, U., Kirchner, J., Schliwa, M., Moroder, L., & Woehlke, G. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg036 · Cited by 22 · see citing works
The structural switch of nucleotide-free kinesin
Cao, L., Cantos-Fernandes, S., & Gigant, B. (2017) · Scientific Reports · doi:10.1038/srep42558 · Cited by 20 · see citing works
Fluorescence tools to measure helicase activity in real time.
Toseland, C., & Webb, M. (2010) · Methods · doi:10.1016/j.ymeth.2010.02.012 · Cited by 23
The ATPase Cross-bridge Cycle of the Kar3 Motor Domain
Mackey, A. T., & Gilbert, S. P. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m206219200 · Cited by 21 · see citing works
Nucleotide-Dependent Interaction of the N-Terminal Domain of MukB with Microtubules
Lockhart, A., & Kendrick‐Jones, J. (1998) · Journal of Structural Biology · doi:10.1006/jsbi.1998.4056 · Cited by 17 · see citing works
Chakraborty, S., & Zheng, W. (2014) · Biochemistry · doi:10.1021/bi501056h · Cited by 23 · see citing works
Li, M., & Zheng, W. (2012) · Biochemistry · doi:10.1021/bi300362a · Cited by 21 · see citing works
Mechanistic Analysis of the Saccharomyces cerevisiae Kinesin Kar3*
Mackey, A. T., Sproul, L. R., Sontag, C., Satterwhite, L. L., Correia, J., & Gilbert, S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406268200 · Cited by 19 · see citing works
The luminal Ca2+ transient controls Ca2+ release/re-uptake of sarcoplasmic reticulum.
Ikemoto, N., & Yamamoto, T. (2000) · Biochemical and Biophysical Research Communications - BBRC · doi:10.1006/bbrc.2000.4031 · Cited by 18
The role of thermal activation in motion and force generation by molecular motors
Astumian, R. D. (2000) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2000.0592 · Cited by 23 · see citing works
Models of protein linear molecular motors for dynamic nanodevices
Fulga, F., Nicolau, D. V., & Nicolau, D. V. (2008) · Integrative Biology · doi:10.1039/b814985b · Cited by 18 · see citing works
Theoretical formalism for kinesin motility I. Bead movement powered by single one-headed kinesins.
Chen, Y.-D. (2000) · Biophysical Journal · doi:10.1016/s0006-3495(00)76594-5 · Cited by 15 · see citing works
“25 gives a rate of 53.4 s21, which is very close to the experimental value of 60 s21 found for one-headed kinesin motors by Ma and Taylor (1997a).”
BackgroundMethodInfluentialModulation of the Kinesin ATPase Cycle by Neck Linker Docking and Microtubule Binding
Zhao, P. Y., Kull, F. J., & Cochran, J. C. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.123067 · Cited by 19 · see citing works
Formation and characterization of kinesin.ADP.fluorometal complexes.
Shibuya, H., Kondo, K., Kimura, N., & Maruta, S. (2002) · Journal of Biochemistry (Tokyo) · doi:10.1093/oxfordjournals.jbchem.a003259 · Cited by 14 · see citing works
A Kinesin Mutation That Uncouples Motor Domains and Desensitizes the γ-Phosphate Sensor*
Brendza, K., Sontag, C., Saxton, W., & Gilbert, S. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m001124200 · Cited by 14 · see citing works
Zheng, W., & Li, M. (2012) · Biophysical Journal · doi:10.1016/j.bpj.2011.11.2003 · Cited by 9 · see citing works
Neck-Linker Docking Coordinates the Kinetics of Kinesin's Heads
Czövek, A., Szöllősi, G. J., & Derényi, I. (2011) · Biophysical Journal · doi:10.1016/j.bpj.2011.01.039 · Cited by 10 · see citing works
Preparation and characterization of a novel rice plant-specific kinesin.
Umeki, N., Mitsui, T., Umezu, N., Kondo, K., & Maruta, S. (2006) · Journal of Biochemistry (Tokyo) · doi:10.1093/jb/mvj074 · Cited by 10 · see citing works
Kinetic regulation of kinesin’s two motor domains coordinates its stepping along microtubulesPreprint
Niitani, Y., Matsuzaki, K., Jönsson, E., Vale, R. D., & Tomishige, M. (2025) · eLife · doi:10.7554/elife.106228.2 · Cited by 6 · see citing works
“…of the head to/from microtubule is tightly correlated with the ATPase cycle; ADP release stabilizes the microtubule binding of the head, while phosphate release after ATP hydrolysis induces detachment of the head from the microtubule (Gilbert and Johnson, 1994; Ma and Taylor, 1997a; Cross, 2004).”
Properties of the Kinesin-1 motor DdKif3 from Dictyostelium discoideum
Röhlk, C., Rohlfs, M., Leier, S., Schliwa, M., Liu, X., Parsch, J., & Woehlke, G. (2007) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2007.11.001 · Cited by 6 · see citing works
Analysing the ATP turnover cycle of microtubule motors.
Friel, C. T., Bagshaw, C. R., & Howard, J. (2011) · Methods in molecular biology · doi:10.1007/978-1-61779-252-6_13 · Cited by 6 · see citing works
“There are reports of nucleotide-free kinesin remaining active for up to 2 weeks when stored frozen in a high-salt glycerol buffer (17).”
Background4.17 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
Atherton, J., Chegkazi, M. S., Leusciatti, M., Palma, M. D., Peirano, E., Pozzer, L. S., Meli, M., Pasqualato, S., Foran, T., Morra, G., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-61498-3 · Cited by 9 · see citing works
“MT-stimulated ADP releasehas been proposed to bebiphasic, with the fi rstphasebeinginhibitedbyMg 2+18,30,50 .”
A stochastic model for kinesin bidirectional stepping
Yao, X., & Zheng, Y. (2014) · The Journal of Chemical Physics · doi:10.1063/1.4865934 · Cited by 3 · see citing works
Umezu, N., Hanzawa, N., Yamada, M., Kondo, K., Mitsui, T., & Maruta, S. (2011) · Journal of Biochemistry (Tokyo) · doi:10.1093/jb/mvr012 · Cited by 2 · see citing works
Enhanced axonal transport in large vertebrates: KIF5A adaptations in giraffes and pythonsPreprint
Kambara, T., Rao, L., Yamagishi, Y., Ikeda, K., Taniguchi, D., Imasaki, T., Shigematsu, H., Sakai, N., Gennerich, A., Nitta, R., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.05.04.652084 · Cited by 2 · see citing works
Processivity of the monomeric KLP-6 kinesin and a Brownian ratchet model with symmetric potentialsPreprint
Kita, T., Sasaki, K., & Niwa, S. (2024) · bioRxiv · doi:10.1101/2024.08.06.606760 · Cited by 1 · see citing works
“This hydrolysis rate is consistent with a previous study (26) which showed that KLP-6(D458A) has a similar hydrolysis rate to the well-known kinesin-1 motor domain (about 60 /s) (10, 17, 41–43).”
Backgroundstructural basis of kinesin motility
Cao, L.-Y. (2016) · doi:10.70675/07511a25zb9adz47c1z88f6z44259fb7b885 · Cited by 1
Hackney, D., & McGoff, M. (2016) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2016.08.019 · Cited by 1 · see citing works
“Ma and Taylor were able to stabilize isolated human motor domains in an active nucleotide-free conformation by use of 20% glycerol and high salt or by rapid removal of released ADP by apyrase [8,9].”
Synthesis of a novel fluorescent non-nucleotide ATP analogue and its interaction with myosin ATPase.
Tanaka, K., Kimura, T., & Maruta, S. (2011) · Journal of Biochemistry (Tokyo) · doi:10.1093/jb/mvq154 · Cited by 1
Metzler, D., Metzler, C. M., & Sauke, D. J. (2001) · Elsevier eBooks · doi:10.1016/b978-012492543-4/50022-2 · Cited by 1 · see citing works
Kinetic characterisation of microgram quantities of myosins using a novel flash photolysis apparatus
Weiss, S., Goody, R., & Geeves, M. (2002) · doi:10.17877/de290r-8864
Motor proteins of the kinesin superfamily
Hackney, D. D. (2003) · The Enzymes · doi:10.1016/s1874-6047(04)80004-0 · Cited by 1 · see citing works
- Authors
- Ma, Y.-Z., & Taylor, E. W.
- Affiliations
- University of Chicago (US)
- Corresponding author
- Taylor, Edwin W.
- ORCID
- Taylor, Edwin W.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1997-01
- Volume
- 272
- Issue
- 2
- Pages
- 717-723
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2043341507
- Cited by
- 96
- References
- 18
- Citations by year
- 2025: 5 · 2024: 2 · 2017: 2 · 2016: 3 · 2015: 3 · 2014: 4 · 2013: 2 · 2012: 3
- FWCI
- 2.59
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r01gm051858-04)
- National Institute of General Medical Sciences (GM 51858)
- 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 › Molecular Biology › ATP Synthase and ATPases Research
- Keywords
- kinesin, ATPase kinetics, microtubule binding, ADP dissociation, ATP hydrolysis, processivity, kinetic mechanism, rate constants
- MeSH terms
- Adenosine Diphosphate, Adenosine Triphosphate, Animals, Cattle, Dose-Response Relationship, Drug, Humans, Kinetics, Microtubules, Protein Conformation, Spectrometry, Fluorescence, Kinesins
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