Characterization of α2β2 and α2 forms of kinesin
Abstract
Bovine brain kinesin separates into two components on sucrose density gradient centrifugation. The predominant component is a heterotetramer of two 120 kDa alpha subunits and two 64 kDa beta subunits with an sedimentation coefficient of 9.6 S and a low Vm rate of microtubule-stimulated ATPase of 1.3 +/- 0.5 sec-1 at 25 degrees, pH 7.0. The minor element is a homodimer of two alpha subunits without beta subunits with a sedimentation coefficient of 6.9 S and a higher Vm rate of microtubule-stimulated ATPase of 7.0 +/- 1.9 sec-1. Microtubules stimulate the rate of release of ADP from the active site of the tetramer, but the rate of release is not fast enough to account for the rate of steady state ATP hydrolysis. Further complexity is indicated by biphasic release kinetics. In spite of the large difference in Vm ATPase rate for the two species, both drive the sliding of sea urchin axonemes over glass surfaces at the same velocity.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The proposed role of LC is consistent with previous reports that HC alone has a higher MT-stimulated ATPase activity than HC and LC together.
“The proposed role of LC is also consistent with previous reports that HC alone has a higher MT-stimulated ATPase activity than HC and LC together (Hackney et al., 1991).”
From Light Chain– dependent Regulation of Kinesin's Interaction with Microtubules (1998) · cites this paper as Hackney et al., 1991
Cites
Kuznetsov, S. A., Vaisberg, Y. A., Rothwell, S. W., Murphy, D. B., & Gelfand, V. I. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31301-7 · Cited by 95 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Force and velocity measured for single kinesin molecules
Svoboda, K., & Block, S. M. (1994) · Cell · doi:10.1016/0092-8674(94)90060-4 · Cited by 909 · 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
Self-citationKinesin׳s tail domain is an inhibitory regulator of the motor domain
Coy, D. L., Hancock, W. O., Wagenbach, M., & Howard, J. (1999) · Nature Cell Biology · doi:10.1038/13001 · Cited by 329 · see citing works
Fluctuation analysis of motor protein movement and single enzyme kinetics.
Svoboda, K., Mitra, P. P., & Block, S. M. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.25.11782 · Cited by 294 · see citing works
Light Chain– dependent Regulation of Kinesin's Interaction with Microtubules
Verhey, K. J., Lizotte, D. L., Abramson, T., Barenboim, L., Schnapp, B. J., & Rapoport, T. A. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.143.4.1053 · Cited by 266 · see citing works
“The proposed role of LC is also consistent with previous reports that HC alone has a higher MT-stimulated ATPase activity than HC and LC together (Hackney et al., 1991).”
ResultKinesin Assembly and Movement in Cells
Verhey, K. J., Kaul, N., & Soppina, V. (2011) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-042910-155310 · Cited by 231 · see citing works
Kinesin Light Chains Are Essential for Axonal Transport in <i>Drosophila </i>
Gindhart, J. G., Desai, C. J., Beushausen, S., Zinn, K., & Goldstein, L. S. B. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.141.2.443 · Cited by 179 · see citing works
Kinesin undergoes a 9 S to 6 S conformational transition
Hackney, D. D., Levitt, J. D., & Suhan, J. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42499-4 · Cited by 175 · see citing works
Self-citationHuang, T. G., & Hackney, D. D. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)34033-4 · Cited by 174 · see citing works
Self-citationCloning and localization of a conventional kinesin motor expressed exclusively in neurons
Niclas, J., Navone, F., Hom-Booker, N., & Vale, R. D. (1994) · Neuron · doi:10.1016/0896-6273(94)90314-x · Cited by 153 · see citing works
Immunochemical analysis of kinesin light chain function
Stenoien, D. L., & Brady, S. T. (1997) · Molecular Biology of the Cell · doi:10.1091/mbc.8.4.675 · Cited by 143 · see citing works
Fission yeast pkl1 is a kinesin-related protein involved in mitotic spindle function.
Pidoux, A. L., LeDizet, M., & Cande, W. Z. (1996) · Molecular Biology of the Cell · doi:10.1091/mbc.7.10.1639 · Cited by 115 · see citing works
The carboxyl-terminal domain of kinesin heavy chain is important for membrane binding
Skoufias, D. A., Cole, D. G., Wedaman, K. P., & Scholey, J. M. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42281-2 · Cited by 110 · see citing works
The Drosophila kinesin light chain. Primary structure and interaction with kinesin heavy chain
Gauger, A. K., & Goldstein, L. S. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)38698-3 · Cited by 105 · see citing works
Defective kinesin heavy chain behavior in mouse kinesin light chain mutants
Rahman, A., Kamal, A., Roberts, E. A., & Goldstein, L. S. B. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.146.6.1277 · Cited by 102 · see citing works
Gilbert, S. P., & Johnson, K. A. (1993) · Biochemistry · doi:10.1021/bi00068a028 · Cited by 88 · see citing works
Hackney, D. D. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)34035-8 · Cited by 68 · see citing works
Self-citation
- Authors
- Hackney, D. D., Levitt, J. D., & Wagner, D. D.
- Affiliations
- Carnegie Mellon University (US)
- ORCID
- Hackney, David D.
- Venue
- Biochemical and Biophysical Research Communications
- Publisher
- Elsevier BV
- Published
- 1991-01
- Volume
- 174
- Issue
- 2
- Pages
- 810-815
- ISSN
- 0006-291X (ISSN-L)
- OpenAlex
- W2466189457
- Cited by
- 80
- References
- 1
- Citations by year
- 2026: 3 · 2025: 1 · 2022: 3 · 2021: 1 · 2018: 1 · 2015: 1 · 2013: 1 · 2012: 1
- FWCI
- 2.96
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochemical and Biophysical Research Communications (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of Neurological Disorders and Stroke (NS28562, R01NS028562)
- National Institute of Arthritis and Musculoskeletal and Skin Diseases (AR25980, R01AR025980)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetic and Kidney Cyst Diseases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Keywords
- kinesin, heterotetramer, homodimer, ATP hydrolysis kinetics, sedimentation coefficient, bovine brain
- MeSH terms
- Adenosine Triphosphatases, Animals, Brain, Cattle, Centrifugation, Density Gradient, Chromatography, Gel, Kinetics, Microtubule Proteins, Molecular Weight, Kinesins, Macromolecular Substances
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
