The DOI matches its Crossref record; 31 of the 31 references it cites were found in a registry or an index.
Kinesin undergoes a 9 S to 6 S conformational transition
Open accessAbstract
Addition of NaCl or KCl in the presence of 50 nM ATP induces a shift in the sedimentation coefficient (apparent S20,w) of kinesin from 9.4 S at low ionic strength to 6.5 S at high ionic strength. The midpoint for the transition occurs at ionic strength values of 0.39, 0.25, and 0.18 for pH values of 6.3, 6.9, and 8.3, respectively. Gel filtration experiments indicate that the transition to the 6.5 S species is accompanied by a decrease in the diffusion coefficient. Under all conditions which were tested, the 64-kDa beta subunits comigrate with the 120-kDa alpha subunits without any evidence for dissociation of the alpha 2 beta 2 complex. These results are consistent with the change in sedimentation coefficient being due to a conformational transition between a folded form at low ionic strength and an extended form at high ionic strength. This conformational transition is not significantly affected by the nature of the nucleotide bound at the active site since similar results are obtained both in the presence of excess EDTA, which removes the bound ADP, and after replacement of the bound ADP with adenosine 5'-(beta,gamma-imino)triphosphate. The alpha 2 form of kinesin, which lacks the beta subunits, undergoes a similar transition between a 6.7 S form at low ionic strength and a 5.1 S form at high ionic strength with a midpoint for the transition at an ionic strength of 0.5 at pH 6.9. Electron microscopic observation also indicates a transition between a folded conformation at low ionic strength and an extended conformation at high ionic strength for both the alpha 2 beta 2 and alpha 2 species.
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“At physiological salt concentrations, purified kinesin is in a folded conformation in which the tail comes close to the motor domain, while, in high salt, kinesin is in an extended conformation.”
From Light Chain– dependent Regulation of Kinesin's Interaction with Microtubules (1998) · cites this paper as Hackney et al., 1992
In the citing paper
“Sedimentation in a high salt buffer (0.5 M NaCl) shifted the proteins to an extended 6S conformation at both pH 7.2 and 6.8 (Fig. 8 D), in agreement with the data obtained for purified kinesin (Hackney et al., 1992).”
From Light Chain– dependent Regulation of Kinesin's Interaction with Microtubules (1998) · cites this paper as Hackney et al., 1992
In the citing paper
“At both pH values, the proteins sedimented at ∼9S (Fig. 8 D), corresponding to the folded conformation of kinesin in which the tail and motor domains are in proximity to each other (Hackney et al., 1992).”
From Light Chain– dependent Regulation of Kinesin's Interaction with Microtubules (1998) · cites this paper as Hackney et al., 1992
In the citing paper
“Indeed, the sedimentation coefficient of 9S determined for kinesin in cell lysates corresponds to the folded conformation of purified kinesin as determined by sedimentation and electron microscopy analysis (Hirokawa et al., 1989; Hisanaga et al., 1989; Hackney et al., 1992).”
From Light Chain– dependent Regulation of Kinesin's Interaction with Microtubules (1998) · cites this paper as Hackney et al., 1992
Citations
Cites
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961
Substructure of the myosin molecule
Weeds, A. G., & Lowey, S. (1971) · Journal of Molecular Biology · doi:10.1016/0022-2836(71)90074-x · Cited by 1,067
[7] Preparation of myosin and its subfragments from rabbit skeletal muscle
Margossian, S. S., & Lowey, S. (1982) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(82)85009-x · Cited by 981
Substructure of the myosin molecule
Lowey, S., Slayter, H. S., Weeds, A. G., & Baker, H. (1969) · Journal of Molecular Biology · doi:10.1016/0022-2836(69)90483-5 · Cited by 779
A new protein of the thick filaments of vertebrate skeletal myofibrils
Offer, G., Moos, C., & Starr, R. (1973) · Journal of Molecular Biology · doi:10.1016/0022-2836(73)90055-7 · Cited by 629
Hirokawa, N., Pfister, K. K., Yorifuji, H., Wagner, M. C., Brady, S. T., & Bloom, G. S. (1989) · Cell · doi:10.1016/0092-8674(89)90691-0 · Cited by 477
A New Calibration Procedure for Gel Filtration Columns
Ackers, G. K. (1967) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)95955-7 · Cited by 413
Yang, J. T., Laymon, R. A., & Goldstein, L. S. B. (1989) · Cell · doi:10.1016/0092-8674(89)90692-2 · Cited by 395
A bent monomeric conformation of myosin from smooth muscle.
Trybus, K. M., Huiatt, T. W., & Lowey, S. (1982) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.79.20.6151 · Cited by 300
Bloom, G. S., Wagner, M. C., Pfister, K. K., & Brady, S. T. (1988) · Biochemistry · doi:10.1021/bi00409a043 · Cited by 284
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Manning, B. D., & Snyder, M. P. (2000) · Trends in Cell Biology · doi:10.1016/s0962-8924(00)01774-8 · Cited by 42
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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
Cloning and functional expression of a `fast' fungal kinesin
Grummt, M., Pistor, S., Lottspeich, F., & Schliwa, M. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)00399-8 · Cited by 27
Cross, R. A., & Scholey, J. M. (1999) · Nature Cell Biology · doi:10.1038/12947 · Cited by 25
Cargo-activated ATPase activity of kinesin.
Jiang, M. Y., & Sheetz, M. P. (1995) · Europe PMC (PubMed Central) · Cited by 24
Mechanisms for regulation of plant kinesins
Ganguly, A., & Dixit, R. (2013) · Current Opinion in Plant Biology · doi:10.1016/j.pbi.2013.09.003 · Cited by 22
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Regulation of kinesin-directed movements
Haimo, L. T. (1995) · Trends in Cell Biology · doi:10.1016/s0962-8924(00)88981-3 · Cited by 22
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Cross, J. A., Dawson, W., Shukla, S., Weijman, J. F., Mantell, J., Dodding, M. P., & Woolfson, D. N. (2024) · Nature Chemical Biology · doi:10.1038/s41589-024-01640-2 · Cited by 19
The mechanics of force generation by kinesin.
Howard, J. (1995) · Europe PMC (PubMed Central) · Cited by 21
Hackney, D. D. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200611082 · Cited by 20
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Martin, M., Hurd, D. D., & Saxton, W. M. (1999) · Cellular and Molecular Life Sciences · doi:10.1007/s000180050422 · Cited by 20
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Wong, Y. L., & Rice, S. E. (2010) · Biophysical Journal · doi:10.1016/j.bpj.2009.12.2000 · Cited by 17
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
Cremo, C. R., & Hartshorne, D. J. (2007) · Springer eBooks · doi:10.1007/978-1-4020-6519-4_6 · Cited by 15
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Khataee, H. R., & Khataee, A. (2010) · NANO · doi:10.1142/s1793292010001792 · Cited by 14
The mechanical properties of kinesin-1: a holistic approach
Jeppesen, G. M., & Hoerber, J. (2012) · Biochemical Society Transactions · doi:10.1042/bst20110768 · Cited by 14
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Watanabe, T. M., Yanagida, T., & Iwane, A. H. (2010) · Biochemistry · doi:10.1021/bi9021582 · Cited by 13
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Single molecule FRET observation of kinesin-1's head-tail interaction on microtubule
Aoki, T., Tomishige, M., & Ariga, T. (2013) · BIOPHYSICS · doi:10.2142/biophysics.9.149 · Cited by 10
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Ferro, K. L., & Collins, C. A. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.9.4492 · Cited by 10
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Walker, R. A., O’Brien, E. T., Epstein, D. L., & Sheetz, M. P. (1997) · Cell Motility and the Cytoskeleton · doi:10.1002/(sici)1097-0169(1997)37:4 · Cited by 8
Howard, J. (1993) · Nature · doi:10.1038/365696b0 · Cited by 7
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Kapitein, L. C., & Peterman, E. J. G. (2009) · Elsevier eBooks · doi:10.1016/b978-0-12-374227-8.00002-x · Cited by 6
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Queen, K. A., Cario, A., Berger, C. L., & Stumpff, J. (2024) · Molecular Biology of the Cell · doi:10.1091/mbc.e23-05-0167 · Cited by 5
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Tan, Z., Missman, A., & Cianfrocco, M. A. (2026) · Biochemical Journal · doi:10.1042/bcj20253135 · Cited by 5
Verhey, K. J., Cochran, J. C., & Walczak, C. (2015) · Springer eBooks · doi:10.1007/978-94-017-9732-0_1 · Cited by 5
Axonal Transport: Imaging and Modeling of a Neuronal Process
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Smith, E. R., Turner, E. D., Abdelhamid, M. A. S., Craggs, T. D., & Twelvetrees, A. E. (2024) · doi:10.1101/2024.12.20.629623 · Cited by 4
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Lee, H., & Plamann, M. D. (2001) · Springer eBooks · doi:10.1007/978-3-662-06101-5_11 · Cited by 4
Schroer, T. A., & Gill, S. R. (1996) · Current topics in membranes · doi:10.1016/s0070-2161(08)60383-4 · Cited by 3
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Prevo, B., Açar, Ş., Kruijssen, D. L. H., & Peterman, E. J. G. (2000) · Wiley eBooks · doi:10.1002/9780470027318.a9267 · Cited by 3
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Self-citationMylonas, S. (2005) · Cited by 1
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Clancy, B. E., & Block, S. M. (2012) · Elsevier eBooks · doi:10.1016/b978-0-12-374920-8.00422-7
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Lluesma, S. M. (2002) · Archive ouverte UNIGE (University of Geneva) · doi:10.13097/archive-ouverte/unige:145
Analysis of mutations in the kinesin motor that decouple ATPase activity and microtubule interaction
Auerbach, S. D. (2004) · Texas ScholarWorks (Texas Digital Library)
Mechanism of the mitotic kinesin CENP-E in tethering kinetochores to spindle microtubules
Kim, Y. (2009) · eScholarship (California Digital Library)
Dynamics of Active and Passive Microtubule-Crosslinking Proteins
Kapitein, L. C. (2007) · Digital Academic REpository of VU University Amsterdam (Vrije Universiteit Amsterdam)
Kinesin-1 Transport Motor Domain Phosphorylation Modulates
Trybus, K. M., Selvin, P. R., Berger, C. L., Lu, Y., Torabi, S. F., Thompson, A. R., DeBerg, A., & Blehm, B. H. (2014)
Fesselin and caldesmon: natively unfolded proteins in smooth muscle regulation
Hamden, S. S. (2010) · The Scholarship East Carolina University's Institutional Repository (East Carolina University)
Phosphorylation-induced structural changes in smooth muscle myosin.
Kast, D. J. E. (2010) · University of Minnesota Digital Conservancy (University of Minnesota)
The regulation of KIF3A motor subunit by phosphorylation
Chen, K. (2018) · DR-NTU (Nanyang Technological University) · doi:10.32657/10356/73335
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Arthur, A. L. (2020) · University of Minnesota Digital Conservancy (University of Minnesota)
The Role of Bicaudal D in motor protein mediated transport
Noordstra, I. (2012) · Utrecht University Repository (Utrecht University)
Amos, L. (2008) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.1119006.576148
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Metadata
- Authors
- Hackney, D. D., Levitt, J. D., & Suhan, J.
- Affiliations
- Carnegie Mellon University (US)
- ORCID
- Hackney, D.D.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1992-04
- Volume
- 267
- Issue
- 12
- Pages
- 8696-8701
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1528749730
- Cited by
- 175
- References
- 31
- Citations by year
- 2026: 4 · 2025: 4 · 2024: 2 · 2023: 1 · 2022: 2 · 2020: 2 · 2019: 1 · 2018: 4 · 2017: 2 · 2016: 2 · 2015: 1 · 2014: 7 · 2013: 9 · 2012: 6
- FWCI
- 3.53
- 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 (5r01ar025980-11)
- National Institute of Neurological Disorders and Stroke (NS28562, R01NS028562)
- National Institute of Arthritis and Musculoskeletal and Skin Diseases (AR25980)
- 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 › Structural Biology › Enzyme Structure and Function
- Keywords
- kinesin, conformational change, ionic strength, sedimentation coefficient, diffusion coefficient, ATP binding, ADP, MgATP, protein folding
- MeSH terms
- Animals, Brain, Cattle, Chromatography, Gel, Electrophoresis, Polyacrylamide Gel, Microscopy, Electron, Osmolar Concentration, Potassium Chloride, Protein Conformation, Sodium Chloride, Kinesins
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