ArticleProceedings of the National Academy of Sciences of the United States of America1993
Direction of microtubule movement is an intrinsic property of the motor domains of kinesin heavy chain and Drosophila ncd protein.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed.
- Structural analysis of a motor with increased mechanical output reveals new transitions in kinesin microtubule motility.Scientific reports · 2026Article
- Article
- The Kinesin-14 tail: Dual microtubule binding domains drive spindle morphogenesis through tight microtubule cross-linking and robust sliding.Molecular biology of the cell · 2025Article
- Tether-scanning the kinesin motor domain reveals a core mechanical action.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- A stop or go switch: glycogen synthase kinase 3β phosphorylation of the kinesin 1 motor domain at Ser314 halts motility without detaching from microtubules.Development (Cambridge, England) · 2021Article
- Automated Multi-Peak Tracking Kymography (AMTraK): A Tool to Quantify Sub-Cellular Dynamics with Sub-Pixel Accuracy.PloS one · 2016Article
- Force generation by kinesin and myosin cytoskeletal motor proteins.Journal of cell science · 2013Review
- Tubulin depolymerization may be an ancient biological motor.Journal of cell science · 2010Review
- In vitro assays to study the tracking of shortening microtubule ends and to measure associated forces.Methods in cell biology · 2010Review
- The mitotic kinesin CENP-E is a processive transport motor.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Two modes of microtubule sliding driven by cytoplasmic dynein.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Article
- The sliding filament model: 1972-2004.The Journal of general physiology · 2004Review
- Rotation of the stalk/neck and one head in a new crystal structure of the kinesin motor protein, Ncd.The EMBO journal · 2003Article
- Bidirectional cooperative motion of molecular motors.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
- Orphan kinesin NOD lacks motile properties but does possess a microtubule-stimulated ATPase activity.Molecular biology of the cell · 2001Article
- Searching for kinesin's mechanical amplifier.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2000Review
- Kinesin's processivity results from mechanical and chemical coordination between the ATP hydrolysis cycles of the two motor domains.Proceedings of the National Academy of Sciences of the United States of America · 1999Article
- Light chain-dependent regulation of Kinesin's interaction with microtubules.The Journal of cell biology · 1998Article
- Importance of a flexible hinge near the motor domain in kinesin-driven motility.The EMBO journal · 1998Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The kinesin heavy chain and the ncd (non-claret disjunctional) gene product of Drosophila are microtubule-associated motor proteins related by sequence similarity within an approximately 340-aa domain. Despite the sequence similarity, the kinesin heavy chain and ncd protein move in opposite directions on microtubules. To investigate the molecular basis for direction of movement, we created a series of truncated kinesin heavy chain and ncd proteins. We found that the conserved domain of both proteins has microtubule motor activity, although the efficiency with which ATP hydrolysis is coupled to microtubule movement declines dramatically with increasing truncation. Further, the direction of movement is intrinsic to the conserved motor domains, rather than being a consequence of domain organization or adjacent sequences.
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