The DOI matches its Crossref record; 12 of the 12 references it cites were found in a registry or an index.
Processivity of the Motor Protein Kinesin Requires Two Heads
Open accessAbstract
A single kinesin molecule can move for hundreds of steps along a microtubule without dissociating. One hypothesis to account for this processive movement is that the binding of kinesin's two heads is coordinated so that at least one head is always bound to the microtubule. To test this hypothesis, the motility of a full-length single-headed kinesin heterodimer was examined in the in vitro microtubule gliding assay. As the surface density of single-headed kinesin was lowered, there was a steep fall both in the rate at which microtubules landed and moved over the surface, and in the distance that microtubules moved, indicating that individual single-headed kinesin motors are not processive and that some four to six single-headed kinesin molecules are necessary and sufficient to move a microtubule continuously. At high ATP concentration, individual single-headed kinesin molecules detached from microtubules very slowly (at a rate less than one per second), 100-fold slower than the detachment during two-headed motility. This slow detachment directly supports a coordinated, hand-over-hand model in which the rapid detachment of one head in the dimer is contingent on the binding of the second head.
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Citations
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
Bead movement by single kinesin molecules studied with optical tweezers
Block, S. M., Goldstein, L. S. B., & Schnapp, B. J. (1990) · Nature · doi:10.1038/348348a0 · Cited by 1,038
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
Direct observation of single kinesin molecules moving along microtubules
Vale, R. D., Funatsu, T., Pierce, D. W., Romberg, L., Harada, Y., & Yanagida, T. (1996) · Nature · doi:10.1038/380451a0 · Cited by 711
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
The Crystal Structure of Dimeric Kinesin and Implications for Microtubule-Dependent Motility
Kozielski, F., Sack, S., Marx, A., Thormählen, M., Schönbrunn, E., Biou, V, Thompson, A., Mandelkow, E.-M., & Mandelkow, E. (1997) · Cell · doi:10.1016/s0092-8674(00)80489-4 · Cited by 408
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
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
Interacting Head Mechanism of Microtubule-Kinesin ATPase
Ma, Y.-Z., & Taylor, E. W. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.2.724 · Cited by 181
Highly processive microtubule-stimulated ATP hydrolysis by dimeric kinesin head domains
Hackney, D. D. (1995) · Nature · doi:10.1038/377448a0 · Cited by 177
Cited by
The Way Things Move: Looking Under the Hood of Molecular Motor Proteins
Vale, R. D., & Milligan, R. A. (2000) · Science · doi:10.1126/science.288.5463.88 · Cited by 1,503
Microtubule Acetylation Promotes Kinesin-1 Binding and Transport
Reed, N. A., Cai, D., Blasius, T. L., Jih, G. T., Meyhofer, E., Gaertig, J., & Verhey, K. J. (2006) · Current Biology · doi:10.1016/j.cub.2006.09.014 · Cited by 919
A structural change in the kinesin motor protein that drives motility
Rice, S., Lin, A. W., Safer, D., Hart, C. L., Naber, N., Carragher, B. O., Cain, S. M., Pechatnikova, E., Wilson-Kubalek, E. M., Whittaker, M., et al. (1999) · Nature · doi:10.1038/45483 · Cited by 798
Myosin-V is a processive actin-based motor
Mehta, A. D., Rock, R. S., Rief, M., Spudich, J. A., Mooseker, M. S., & Cheney, R. E. (1999) · Nature · doi:10.1038/23072 · Cited by 786
Single-Molecule Biomechanics with Optical Methods
Mehta, A. D., Rief, M., Spudich, J. A., Smith, D. A., & Simmons, R. M. (1999) · Science · doi:10.1126/science.283.5408.1689 · Cited by 666
Metadata
- Authors
- Hancock, W. O., & Howard, J.
- Venue
- The Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 1998-03-23
- Volume
- 140
- Issue
- 6
- Pages
- 1395-1405
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- OpenAlex
- W2071777531
- Cited by
- 297
- References
- 12
- FWCI
- 6.90
- Type
- journal article
- Language
- en
- Open access
- green
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
