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Cytoskeletal filaments propelled by surface-bound motor proteins can be viewed as active polymers, a class of active matter. When constraints are imposed on their movements, the propelled cytoskeletal filaments show dynamic patterns distinct from equilibrium conformations. Pinned at their leading ends, propelled microtubules or actin filaments form rotating spirals, whose shape is determined by the interplay between motor forces and the mechanics of the cytoskeletal filaments. We simulated the spiral formations of microtubules propelled by kinesin motors in an overdamped dynamics framework, which in addition to the mechanics of the spiralling microtubule explicitly includes the mechanics of kinesin motors. The simulation revealed that spiral formation was initiated by localized buckling of microtubules near the pinned ends, and the conditions for occurrence of spiral formation were summarized in a phase diagram. The radius of the formed spirals scaled with the surface motor density with an exponent of approximately - 1/4, distinct from previous theoretical and simulation studies based on implicit modelling of motor proteins. This result can be understood as a consequence of the contributions of kinesin motors to the total elastic deformation energy, highlighting the importance of mechanics of motor proteins in the behaviour of the active polymers. These findings can be useful in accurate modelling of active polymers and in designing active polymer-based applications such as molecular shuttles driven by motor proteins.
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http://dx.doi.org/10.1038/s41598-025-03384-y | DOI Listing |
Curr Biol
September 2025
Department of Molecular and Cellular Biology, University of California, 1 Shields Avenue, Davis, CA 95616, USA. Electronic address:
Nuclear migration plays a fundamental role in development, requiring precise spatiotemporal control of bidirectional movement through dynein and kinesin motors. Here, we uncover a differential isoform-dependent mechanism for developmental regulation of nuclear migration directionality. The nuclear envelope Klarsicht/ANC-1/Syne homology (KASH) protein UNC-83 in Caenorhabditis elegans exists in multiple isoforms that differentially control motor activity to achieve tissue-specific nuclear positioning.
View Article and Find Full Text PDFJ Cell Biol
October 2025
Department of Cell and Developmental Biology, University of Colorado Anschutz Medical Campus, Aurora, CO, USA.
Carboxy-terminal tails (CTTs) of tubulin proteins are sites of regulating microtubule function. We previously conducted a genetic interaction screen and identified Kip3, a kinesin-8 motor, as potentially requiring the β-tubulin CTT (β-CTT) for function. Here we use budding yeast to define how β-CTT promotes Kip3 function and the features of β-CTT that are important for this mechanism.
View Article and Find Full Text PDFbioRxiv
August 2025
Department of Biochemistry and Gruss-Lipper Biophotonics Center, Albert Einstein College of Medicine, Bronx, NY 10461, USA.
Pathogenic variants in the motor domain of the kinesin-3 motor protein KIF1A cause a range of neurodevelopmental and neurodegenerative conditions collectively termed KIF1A-associated neurological disorder (KAND). Among these, mutations at residue R350 are linked to hereditary spastic paraplegia and altered motor function. Yet, the structural basis for their pathogeny remains unclear.
View Article and Find Full Text PDFKinesin-1 is a robust motor that carries intracellular cargos towards the plus ends of microtubules. However, optical trapping studies reported that kinesin-1 is a slippery motor that quickly detaches from the microtubule, and multiple kinesins are incapable of teaming up to generate large collective forces. This may be due to the vertical (z) forces that the motor experiences in a single bead trapping assay, accelerating the detachment of the motor from a microtubule.
View Article and Find Full Text PDFStructure
September 2025
Department of Biomedical and Molecular Sciences, Queen's University, Kingston, ON K7L 3N6, Canada. Electronic address:
Kinesin-8 motors regulate kinetochore-microtubule dynamics and control spindle length and positioning. Certain isoforms achieve this by traversing microtubules, accumulating at plus-ends, and depolymerizing terminal αβ-tubulin subunits. While the kinesin-8 motor domain is well characterized, the tail domain regions are less understood.
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