The conformational cycle of kinesin
Open accessAbstract
The stepping mechanism of kinesin can be thought of as a programme of conformational changes. We briefly review protein chemical, electron microscopic and transient kinetic evidence for conformational changes, and working from this evidence, outline a model for the mechanism. In the model, both kinesin heads initially trap Mg x ADP. Microtubule binding releases ADP from one head only (the trailing head). Subsequent ATP binding and hydrolysis by the trailing head progressively accelerate attachment of the leading head, by positioning it closer to its next site. Once attached, the leading head releases its ADP and exerts a sustained pull on the trailing head. The rate of closure of the molecular gate which traps ADP on the trailing head governs its detachment rate. A speculative but crucial coordinating feature is that this rate is strain sensitive, slowing down under negative strain and accelerating under positive strain.
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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 [14]
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
The Crystal Structure of Dimeric Kinesin and Implications for Microtubule-Dependent Motility
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Kinesin Takes One 8-nm Step for Each ATP That It Hydrolyzes
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Coupling of kinesin steps to ATP hydrolysis
Hua, W., Young, E. C., Fleming, M. L., & Gelles, J. (1997) · Nature · doi:10.1038/41118 · Cited by 358 · see citing works
Evidence for alternating head catalysis by kinesin during microtubule-stimulated ATP hydrolysis.
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Determinants of Kinesin Motor Polarity
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“…at least transiently, but the kinetic work shows that binding of the second head in AMPPNP is about tenfold slower than ¢rst-head binding (Ma & Taylor 1997; Gilbert et al. 1998), so that at saturating concentrations of kinesin, one would predict that most sites would become occupied by ¢rst heads.”
BackgroundAlternating 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
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Force production by single kinesin motors
Schnitzer, M. J., Visscher, K., & Block, S. M. (2000) · Nature Cell Biology · doi:10.1038/35036345 · Cited by 572 · 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
Alternate fast and slow stepping of a heterodimeric kinesin molecule
Kaseda, K., Higuchi, H., & Hirose, K. (2003) · Nature Cell Biology · doi:10.1038/ncb1067 · Cited by 179 · see citing works
Self-citationAn ATP Gate Controls Tubulin Binding by the Tethered Head of Kinesin-1
Alonso, M. C., Drummond, D. R., Kain, S., Hoeng, J., Amos, L., & Cross, R. A. (2007) · Science · doi:10.1126/science.1136985 · Cited by 120 · see citing works
Self-citationWhat 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
Self-citationKIF1D 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
Self-citationA mobile kinesin-head intermediate during the ATP-waiting state
Asenjo, A. B., & Sosa, H. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808355106 · Cited by 64 · see citing works
Kinesin’s backsteps under mechanical load
Hyeon, C., Klumpp, S., & Onuchic, J. N. (2009) · Physical Chemistry Chemical Physics · doi:10.1039/b903536b · Cited by 51 · see citing works
- Authors
- Cross, R. A., Crevel, I., Carter, N. J., Alonso, M. C., Hirose, K., & Amos, L. A.
- Affiliations
- Marie Curie (GB)
- MRC Laboratory of Molecular Biology (GB)
- National Institute of Advanced Interdisciplinary Research, Tsukuba 305–8562, Japan
- Corresponding author
- Cross, R. A.
- Venue
- Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences
- Publisher
- The Royal Society
- Published
- 2000-04-29
- Volume
- 355
- Issue
- 1396
- Pages
- 459-464
- ISSN
- 0962-8436 (ISSN-L)
- 1471-2970
- PMC
- PMC1692756
- OpenAlex
- W1981586920
- Cited by
- 39
- References
- 7
- Citations by year
- 2020: 2 · 2019: 1 · 2018: 1 · 2016: 1 · 2015: 1 · 2013: 1 · 2012: 2
- FWCI
- 1.41
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Philosophical Transactions of the Royal Society B Biological 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
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Physical Sciences › Physics and Astronomy › Atomic and Molecular Physics, and Optics › Force Microscopy Techniques and Applications
- Keywords
- kinesin, conformational cycle, microtubule binding, ATP hydrolysis, molecular gates, strain sensitivity, microtubule motor proteins
- MeSH terms
- Adenosine Diphosphate, Adenosine Triphosphate, Animals, Humans, Models, Molecular, Protein Conformation, Kinesins
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