ArticleCurrent biology : CB2022
A kinesin-1 variant reveals motor-induced microtubule damage in cells.
Article in Current biology : CB, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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26 citing papers in PubMed, 49 citations in OpenAlex.
- Article
- Post-Translational Modifications of Tubulin in Oocyte Maturation and Female Infertility.Cytoskeleton (Hoboken, N.J.) · 2026Review
- CLASP2 promotes repair of kinesin-1 damage to the microtubule lattice.bioRxiv : the preprint server for biology · 2026Article
- Microtubule lattice conformation and integrity regulate α-tubulin acetylation.Communications biology · 2026Article
- Tubulin flux at spastin-induced nanodamage sites regulates microtubule rescue frequency and EB1 lifetimes.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Kinesin-Induced Buckling Reveals the Limits of Microtubule Self-Repair.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Mechanical force locally damages, remodels, and stabilizes the lattice of spindle microtubules.Current biology : CB · 2026Article
- SSNA1 mechanically reinforces the damaged microtubule lattice.bioRxiv : the preprint server for biology · 2026Article
- Purification, Fluorescent Labeling, and Detyrosination of Mammalian Cell Tubulin for Biochemical Assays.Cytoskeleton (Hoboken, N.J.) · 2025Article
- Factors Determining Kinesin Motors in a Predominant One-Head-Bound or Two-Heads-Bound State During Its Stepping Cycle.Biomolecules · 2025Article
- Structural switching of tubulin in the microtubule lattice.Biochemical Society transactions · 2025Review
- Mechanism and regulation of kinesin motors.Nature reviews. Molecular cell biology · 2025Review
- Microtubule shaft integrity emerges as a crucial determinant of the acetylation pattern.Cytoskeleton (Hoboken, N.J.) · 2025Article
- Kinesin-1-transported liposomes prefer to go straight in 3D microtubule intersections by a mechanism shared by other molecular motors.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Damage-repair events increase the instability of cortical microtubules in Arabidopsis.Molecular biology of the cell · 2024Article
- Microtubule damage shapes the acetylation gradient.Nature communications · 2024Article
- Insect Cell-Based Expression of Cytoskeletal Motor Proteins for Single-Molecule Studies.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Microtubule acetylation dyshomeostasis in Parkinson's disease.Translational neurodegeneration · 2023Review
- Kinesin-1 autoinhibition facilitates the initiation of dynein cargo transport.The Journal of cell biology · 2023Article
- Causes, costs and consequences of kinesin motors communicating through the microtubule lattice.Journal of cell science · 2023Article
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8 authors at 2 institutions in 1 country.
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Abstract
Kinesins drive the transport of cellular cargoes as they walk along microtubule tracks; however, recent work has suggested that the physical act of kinesins walking along microtubules can stress the microtubule lattice. Here, we describe a kinesin-1 KIF5C mutant with an increased ability to generate damage sites in the microtubule lattice as compared with the wild-type motor. The expression of the mutant motor in cultured cells resulted in microtubule breakage and fragmentation, suggesting that kinesin-1 variants with increased damage activity would have been selected against during evolution. The increased ability to damage microtubules is not due to the enhanced motility properties of the mutant motor, as the expression of the kinesin-3 motor KIF1A, which has similar single-motor motility properties, also caused increased microtubule pausing, bending, and buckling but not breakage. In cells, motor-induced microtubule breakage could not be prevented by increased α-tubulin K40 acetylation, a post-translational modification known to increase microtubule flexibility. In vitro, lattice damage induced by wild-type KIF5C was repaired by soluble tubulin and resulted in increased rescues and overall microtubule growth, whereas lattice damage induced by the KIF5C mutant resulted in larger repair sites that made the microtubule vulnerable to breakage and fragmentation when under mechanical stress. These results demonstrate that kinesin-1 motility causes defects in and damage to the microtubule lattice in cells. While cells have the capacity to repair lattice damage, conditions that exceed this capacity result in microtubule breakage and fragmentation and may contribute to human disease.
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