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| http://dx.doi.org/10.1016/j.cub.2023.04.030 | DOI Listing |
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Impact of physiological ionic strength and crowding on kinesin-1 motility.
Cell Struct Funct
January 2025
Department of Cell Biology, Graduate School of Medical Sciences, Tokushima University.
The motility of biological molecular motors has typically been analyzed by in vitro reconstitution systems using motors isolated and purified from organs or expressed in cultured cells. The behavior of biomolecular motors within cells has frequently been reported to be inconsistent with that observed in reconstituted systems in vitro. Although this discrepancy has been attributed to differences in ionic strength and intracellular crowding, understanding how such parameters affect the motility of motors remains challenging.
View Article and Find Full Text PDFKIF1C activates and extends dynein movement through the FHF cargo adapter.
Nat Struct Mol Biol
January 2025
Centre for Mechanochemical Cell Biology and Warwick Biomedical Sciences, Warwick Medical School, University of Warwick, Coventry, UK.
Cellular cargos move bidirectionally on microtubules by recruiting opposite polarity motors dynein and kinesin. These motors show codependence, where one requires the activity of the other, although the mechanism is unknown. Here we show that kinesin-3 KIF1C acts as both an activator and a processivity factor for dynein, using in vitro reconstitutions of human proteins.
View Article and Find Full Text PDFTotal Internal Reflection Fluorescence (TIRF) Single-Molecule Assay to Analyze the Motility of Kinesin.
Bio Protoc
December 2024
Graduate School of Life Sciences, Tohoku University, Miyagi, Japan.
The motile parameters of kinesin superfamily proteins are fundamental to intracellular transport. Single-molecule motility assays using total internal reflection fluorescence (TIRF) microscopy are a gold standard technique for measuring the motile parameters of kinesin motors. With this technique, one can evaluate the velocity, run length, and binding frequency of kinesins on microtubules by directly observing their motility.
View Article and Find Full Text PDFSelective regulation of kinesin-5 function by β-tubulin carboxy-terminal tails.
J Cell Biol
March 2025
Department of Cell and Developmental Biology, University of Colorado Anschutz Medical Campus, Aurora, CO, USA.
The tubulin code hypothesis predicts that tubulin tails create programs for selective regulation of microtubule-binding proteins, including kinesin motors. However, the molecular mechanisms that determine selective regulation and their relevance in cells are poorly understood. We report selective regulation of budding yeast kinesin-5 motors by the β-tubulin tail.
View Article and Find Full Text PDFDuring cell division, NuMA orchestrates the focusing of microtubule minus-ends in spindle poles and cortical force generation on astral microtubules by interacting with dynein motors, microtubules, and other cellular factors. Here we used in vitro reconstitution, cryo-electron microscopy, and live cell imaging to understand the mechanism and regulation of NuMA. We determined the structure of the processive dynein/dynactin/NuMA complex (DDN) and showed that the NuMA N-terminus drives dynein motility in vitro and facilitates dynein-mediated transport in live cells.
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