ArticleBiophysical journal2009
Pressure-induced changes in the structure and function of the kinesin-microtubule complex.
Article in Biophysical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed.
- The impact of tumor microenvironment: unraveling the role of physical cues in breast cancer progression.Cancer metastasis reviews · 2024Review
- High hydrostatic pressure induces slow contraction in mouse cardiomyocytes.Biophysical journal · 2022Article
- Molecular cancer cell responses to solid compressive stress and interstitial fluid pressure.Cytoskeleton (Hoboken, N.J.) · 2021Review
- High hydrostatic pressure induces vigorous flagellar beating in Chlamydomonas non-motile mutants lacking the central apparatus.Scientific reports · 2020Article
- Kinetic regulation of multi-ligand binding proteins.BMC systems biology · 2016Article
- Review
- Single-molecule analysis of the rotation of F₁-ATPase under high hydrostatic pressure.Biophysical journal · 2013Article
- High hydrostatic pressure induces counterclockwise to clockwise reversals of the Escherichia coli flagellar motor.Journal of bacteriology · 2013Article
- Microscopic analysis of bacterial motility at high pressure.Biophysical journal · 2012Article
- Bacterial motility measured by a miniature chamber for high-pressure microscopy.International journal of molecular sciences · 2012Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Kinesin-1 is an ATP-driven molecular motor that "walks" along a microtubule by working two heads in a "hand-over-hand" fashion. The stepping motion is well-coordinated by intermolecular interactions between the kinesin head and microtubule, and is sensitively changed by applied forces. We demonstrate that hydrostatic pressure works as an inhibitory action on kinesin motility. We developed a high-pressure microscope that enables the application of hydrostatic pressures of up to 200 MPa (2000 bar). Under high-pressure conditions, taxol-stabilized microtubules were shortened from both ends at the same speed. The sliding velocity of kinesin motors was reversibly changed by pressure, and reached half-maximal value at approximately 100 MPa. The pressure-velocity relationship was very close to the force-velocity relationship of single kinesin molecules, suggesting a similar inhibitory mechanism on kinesin motility. Further analysis showed that the pressure mainly affects the stepping motion, but not the ATP binding reaction. The application of pressure is thought to enhance the structural fluctuation and/or association of water molecules with the exposed regions of the kinesin head and microtubule. These pressure-induced effects could prevent kinesin motors from completing the stepping motion.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.