ArticleBiophysical journal1996
Fluctuation in the microtubule sliding movement driven by kinesin in vitro.
Article in Biophysical journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 31 citations in OpenAlex.
- Fluctuation in the Sliding Movement of Kinesin-Driven Microtubules Is Regulated Using the Deep-Sea Osmolyte TrimethylamineACS omega · 2022Article
- Polarity sorting of axonal microtubules: a computational study.Molecular biology of the cell · 2017Article
- A nonequilibrium power balance relation for analyzing dissipative filament dynamics.The European physical journal. E, Soft matter · 2015Article
- Analysis of video-based microscopic particle trajectories using Kalman filtering.Biophysical journal · 2010Article
- Fluctuation of actin sliding over myosin thick filamentsBiophysics (Nagoya-shi, Japan) · 2005Article
- Controlling kinesin by reversible disulfide cross-linking. Identifying the motility-producing conformational change.The Journal of cell biology · 2000Article
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Authors and funding
3 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
We studied the fluctuation in the translational sliding movement of microtubules driven by kinesin in a motility assay in vitro. By calculating the mean-square displacement deviation from the average as a function of time, we obtained motional diffusion coefficients for microtubules and analyzed the dependence of the coefficients on microtubule length. Our analyses suggest that 1) the motional diffusion coefficient consists of the sum of two terms, one that is proportional to the inverse of the microtubule length (as the longitudinal diffusion coefficient of a filament in Brownian movement is) and another that is independent of the length, and 2) the length-dependent term decreases with increasing kinesin concentration. This latter term almost vanishes within the length range we studied at high kinesin concentrations. From the length-dependence relationship, we evaluated the friction coefficient for sliding microtubules. This value is much larger than the solvent friction and thus consistent with protein friction. The length independence of the motional diffusion coefficient observed at sufficiently high kinesin concentrations indicates the presence of correlation in the sliding movement fluctuation. This places significant constraint on the possible mechanisms of the sliding movement generation by kinesin motors in vitro.
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