Kinesin–microtubule binding depends on both nucleotide state and loading direction
Open accessAbstract
Kinesin is a motor protein that transports organelles along a microtubule toward its plus end by using the energy of ATP hydrolysis. To clarify the nucleotide-dependent binding mode, we measured the unbinding force for one-headed kinesin heterodimers in addition to conventional two-headed kinesin homodimers under several nucleotide states. We found that both a weak and a strong binding state exist in each head of kinesin corresponding to a small and a large unbinding force, respectively; that is, weak for the ADP state and strong for the nucleotide-free and adenosine 5′-[β,γ-imido]triphosphate states. Model analysis showed that ( i ) the two binding modes in each head could be explained by a difference in the binding energy and ( ii ) the directional instability of binding, i.e., dependence of unbinding force on loading direction, could be explained by a difference in the characteristic distance for the kinesin–microtubule interaction during plus- and minus-end-directed loading. Both these factors must play an important role in the molecular mechanism of kinesin motility.
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Adding ADP to the AMPPNP-bound kinesin-microtubule system causes one of the two heads to dissociate, leaving one head strongly bound.
“Furthermore, adding ADP to this system will cause one of the two heads to dissociate, leaving one head strongly bound, as illustrated in theright half of Fig. 7A (29”
From Stepping and Stretching (2003) · cites this paper as [29]
The introductory passage (page unavailable) says that kinesin binds with one head when ADP and AMP-PNP coexist, versus two heads with AMP-PNP alone. Results and Discussion (page unavailable) describes AMP-PNP binding as strong. The paper does not establish the claimed sequence—that adding ADP to an already AMP-PNP-bound system causes one head to dissociate. (LLM, conf=0.84)
Experimental — accuracy not yet measuredAMPPNP leads to strong binding of both heads to the microtubule.
“and leads to strong binding of both heads to the microtubule (29”
From Stepping and Stretching (2003) · cites this paper as [29]
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Cites
Direct observation of kinesin stepping by optical trapping interferometry
Svoboda, K., Schmidt, C. F., Schnapp, B. J., & Block, S. M. (1993) · Nature · doi:10.1038/365721a0 · Cited by 1,910 · 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
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Block, S. M. (2007) · Biophysical Journal · doi:10.1529/biophysj.106.100677 · Cited by 338 · 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
How kinesin waits between steps
Mori, T., Vale, R. D., & Tomishige, M. (2007) · Nature · doi:10.1038/nature06346 · Cited by 171 · see citing works
Backsteps 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
Kinesin: world's tiniest biped
Asbury, C. L. (2005) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2004.12.002 · Cited by 116 · 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
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
- Authors
- Uemura, S., Kawaguchi, K., Yajima, J., Edamatsu, M., Toyoshima, Y. Y., & Ishiwata, S.
- Affiliations
- Waseda University (JP)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2002-04-16
- Volume
- 99
- Issue
- 9
- Pages
- 5977-5981
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC122887
- OpenAlex
- W2151130369
- Cited by
- 143
- References
- 2
- Citations by year
- 2026: 5 · 2025: 7 · 2024: 5 · 2023: 6 · 2022: 3 · 2021: 5 · 2020: 6 · 2019: 5 · 2018: 7 · 2017: 5 · 2016: 4 · 2015: 8 · 2014: 5 · 2013: 3 · 2012: 2
- FWCI
- 2.07
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Physical Sciences › Physics and Astronomy › Atomic and Molecular Physics, and Optics › Force Microscopy Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Keywords
- kinesin, microtubule binding, nucleotide state, unbinding force, loading direction, motor protein motility, ATP hydrolysis, binding energy
- MeSH terms
- Adenosine Diphosphate, Animals, Brain, Cattle, Microtubules, Models, Biological, Protein Binding, Stress, Mechanical, Swine, Temperature, Time Factors, Kinesins, Dimerization
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