ArticleThe Journal of general physiology2007
Two distinct modes of processive kinesin movement in mixtures of ATP and AMP-PNP.
Article in The Journal of general physiology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- Quantification of Spatial Patterns of Microtubule Transport by Kinesin-1 Head and Tail.Bio-protocol · 2026Article
- Heterogeneous distribution of kinesin-streptavidin complexes revealed by mass photometry.Soft matter · 2024Article
- The kinesin-5 tail and bipolar minifilament domains are the origin of its microtubule crosslinking and sliding activity.Molecular biology of the cell · 2023Article
- Article
- Cytoskeletal regulation of a transcription factor by DNA mimicry via coiled-coil interactions.Nature cell biology · 2022Article
- Kinesin-14 motors participate in a force balance at microtubule plus-ends to regulate dynamic instability.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Programmed mechano-chemical coupling in reaction-diffusion active matter.Science advances · 2021Article
- Tuning the Properties of Active Microtubule Networks by Depletion Forces.Langmuir : the ACS journal of surfaces and colloids · 2021Article
- Machine learning active-nematic hydrodynamics.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- High-efficacy subcellular micropatterning of proteins using fibrinogen anchors.The Journal of cell biology · 2021Article
- Tunable corrugated patterns in an active nematic sheet.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Flagella-like Beating of a Single Microtubule.Nano letters · 2019Article
- Statistical properties of autonomous flows in 2D active nematics.Soft matter · 2019Article
- Active nematic emulsions.Science advances · 2018Article
- Taming active turbulence with patterned soft interfaces.Nature communications · 2017Article
- Article
- Control of active liquid crystals with a magnetic field.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Article
- Oatp1a1 requires PDZK1 to traffic to the plasma membrane by selective recruitment of microtubule-based motor proteins.Drug metabolism and disposition: the biological fate of chemicals · 2014Article
- Kar3Vik1 mechanochemistry is inhibited by mutation or deletion of the C terminus of the Vik1 subunit.The Journal of biological chemistry · 2013Article
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Abstract
An enzyme is frequently conceived of as having a single functional mechanism. This is particularly true for motor enzymes, where the necessity for tight coupling of mechanical and chemical cycles imposes rigid constraints on the reaction pathway. In mixtures of substrate (ATP) and an inhibitor (adenosine 5'-(beta,gamma-imido)triphosphate or AMP-PNP), single kinesin molecules move on microtubules in two distinct types of multiple-turnover "runs" that differ in their susceptibility to inhibition. Longer (less susceptible) runs are consistent with movement driven by the alternating-sites mechanism previously proposed for uninhibited kinesin. In contrast, kinesin molecules in shorter runs step with AMP-PNP continuously bound to one of the two active sites of the enzyme. Thus, in this mixture of substrate and inhibitor, kinesin can function as a motor enzyme using either of two distinct mechanisms. In one of these, the enzyme can accomplish high-duty-ratio processive movement without alternating-sites ATP hydrolysis.
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