Measuring Kinesin's First Step
Open accessAbstract
A variety of models have recently emerged to explain how the molecular motor kinesin is able to maintain processive movement for over 100 steps. Although these models differ in significant features, they all predict that kinesin's catalytic domains intermittently separate from each other as the motor takes 8-nm steps along the microtubule. Furthermore, at some point in this process, one molecule of ATP is hydrolyzed per step. However, exactly when hydrolysis and product release occur in relation to this forward step have not been established. Furthermore, the rate at which this separation occurs as well as the speed of motor stepping onto and release from the microtubule have not been measured. In the absence of this information, it is difficult to critically evaluate competing models of kinesin function. We have addressed this issue by developing spectroscopic probes whose fluorescence is sensitive to motor-motor separation or microtubule binding. The kinetics of these fluorescence changes allow us to directly measure how fast kinesin steps onto and releases from the microtubule and provide insight into how processive movement is maintained by this motor.
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Kinetic characterizations of K349 and K413 show that only one step in the mechanochemical cycle is affected: the rate of ADP-induced dissociation, which is accelerated 19-fold compared with wild-type.
“Our kinetic characterizations of K349 and K413 has shown that only one step in the mechanochemical cycle is affected (18, 23, and this work). This is the rate of ADP-induced dissociation, which is accelerated 19-fold compared with wild-type (Fig. 4).”
From Stepping and Stretching (2003) · cites this paper as [18]
The Discussion says mutagenesis accelerated ADP-induced release from microtubules while having little effect on ATPase activity or processivity. The Measurement of ATPase Activity and Processivity section reports that this release was approximately 7–8-fold faster than in native kinesin, not 19-fold, and does not establish that no other mechanochemical step was affected. (LLM, conf=0.88)
Experimental — accuracy not yet measuredAMPPNP leads to immobilization of both neck linkers.
“and to immobilization of both neck linkers (18”
From Stepping and Stretching (2003) · cites this paper as [18]
Adding AMPPNP to a kinesin-microtubule complex induces the two neck linkers to separate from each other, similar to what is seen when kinesin takes a forward step with ATP binding.
“Adding AMPPNP to a kinesin-microtubule complex induces the two neck linkers to separate from each other, in a manner similar to what is seen when kinesin takes a forward step with ATP binding (18”
From Stepping and Stretching (2003) · cites this paper as [18]
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Locking Function of a Key Residue in Kinesin's Gating Mechanism
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Optical Spectroscopy of Hydrophobic Sunscreen Molecules Adsorbed to Dielectric Nanospheres¶
Krishnan, R., Carr, A., Blair, E. A., & Nordlund, T. M. (2004) · Photochemistry and Photobiology · doi:10.1111/j.1751-1097.2004.tb01272.x · Cited by 4 · see citing works
Photophysics of single-molecule probes
Levitus, M. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-816463-1.00001-8 · Cited by 3 · see citing works
Anchor Effect of Interactions Between Kinesin’s Nucleotide-Binding Pocket and Microtubule
Jin, Y., Geng, Y.-Z., Lü, L., Ma, Y., Lü, G., Zhang, H., & Ji, Q. (2017) · Cellular and Molecular Bioengineering · doi:10.1007/s12195-017-0477-8 · Cited by 3 · see citing works
Fluorescence microscopy applied to intracellular transport by microtubule motors
Pathak, D., Thakur, S., & Mallik, R. (2018) · Journal of Biosciences · doi:10.1007/s12038-018-9765-2 · Cited by 2 · see citing works
“The neck linker for kinesin was fluorescently labelled with 1,5-IAEDANS to study mechano-chemistry of kinesin between microtubule-associated tryptophans and AEDANS (Rosenfeld et al. 2002).”
MethodKinetic and statistical mechanical modeling of DNA unzipping and kinesin mechanochemistry
Herskowitz, L. (2011) · UNM’s Digital Repository (University of New Mexico) · Cited by 1 · see citing works
Rectified Brownian motion in biology
Mather, W. (2007) · SMARTech Repository (Georgia Institute of Technology) · Cited by 1 · see citing works
Conformation of Troponin and Myosin in Muscle Contraction
Song, L. (2005) · Cited by 1 · see citing works
“The mechanisms resulting in the motility of kinesins such as the hydrolysis of ATP in kinesin stepping (54, 122-131), the interactions of kinesin and microtubule tracks (132), the stepping along microtubules (133, 134) and autoregulation of kinesin activity (38, 135-137) have been studied using FRET approaches (112).”
MethodInfluence of the presence of tubulin C-terminal tail on kinesin-1’s microtubule binding rate
Lipska, A. G., Narayanareddy, B. R. J., Czaplewski, C. R., Sieradzan, A. K., Ocetkiewicz, K. M., Proficz, J., Czarnul, P., Krawczyk, H., Gross, S. P., & Liwo, A. (2026) · Biophysical Journal · doi:10.1016/j.bpj.2026.07.005
- Authors
- Rosenfeld, S. S., Xing, J., Jefferson, G. M., Cheung, H. C., & King, P. H.
- Affiliations
- University of Alabama at Birmingham (US)
- Corresponding author
- Rosenfeld, Steven S.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2002-09
- Volume
- 277
- Issue
- 39
- Pages
- 36731-36739
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2000315199
- Cited by
- 54
- References
- 42
- Citations by year
- 2026: 1 · 2023: 1 · 2021: 2 · 2020: 1 · 2019: 2 · 2018: 3 · 2017: 2 · 2016: 1 · 2015: 3 · 2014: 3 · 2013: 1 · 2012: 2
- FWCI
- 2.31
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- University of Pittsburgh
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biophysics › Advanced Fluorescence Microscopy Techniques
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- kinesin, microtubule binding, ATP hydrolysis, step kinetics, fluorescent probes, microtubule motor proteins
- MeSH terms
- Adenosine Diphosphate, Adenosine Triphosphatases, Adenosine Triphosphate, Animals, Cysteine, Dose-Response Relationship, Drug, Energy Transfer, Fluorescent Dyes, Hydrolysis, Kinetics, Ligands, Microtubules, Models, Biological, Models, Molecular, Mutation, Potassium Chloride, Protein Binding, Spectrometry, Fluorescence, Spectrophotometry, Time Factors, Kinesins, Anisotropy, Protein Structure, Tertiary, Dimerization, Rats
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