ArticleThe Journal of biological chemistry2008
Diffusion and directed movement: in vitro motile properties of fission yeast kinesin-14 Pkl1.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed.
- In vitro reconstitution defines the mechanistic basis of HSET motor activity regulation by IntraFlagellar Transport proteins.Communications biology · 2026Article
- The Kinesin-14 tail: Dual microtubule binding domains drive spindle morphogenesis through tight microtubule cross-linking and robust sliding.Molecular biology of the cell · 2025Article
- Mechanism and regulation of kinesin motors.Nature reviews. Molecular cell biology · 2025Review
- Biased movement of monomeric kinesin-3 KLP-6 explained by a symmetric Brownian ratchet model.Biophysical journal · 2025Article
- Kinesin-14 HSET and KlpA are non-processive microtubule motors with load-dependent power strokes.Nature communications · 2024Article
- Regulation of ciliary homeostasis by intraflagellar transport-independent kinesins.Cell death & disease · 2024Review
- Review
- Mapping the kinetochore MAP functions required for stabilizing microtubule attachments to chromosomes during metaphase.Cytoskeleton (Hoboken, N.J.) · 2019Review
- Pivoting of microtubules driven by minus-end-directed motors leads to spindle assembly.BMC biology · 2019Article
- Suppressor Analysis Uncovers That MAPs and Microtubule Dynamics Balance with the Cut7/Kinesin-5 Motor for Mitotic Spindle Assembly inG3 (Bethesda, Md.) · 2019Article
- The mitotic kinesin-14 KlpA contains a context-dependent directionality switch.Nature communications · 2017Article
- Motile properties of the bi-directional kinesin-5 Cin8 are affected by phosphorylation in its motor domain.Scientific reports · 2016Article
- Loss of kinesin-14 results in aneuploidy via kinesin-5-dependent microtubule protrusions leading to chromosome cut.Nature communications · 2015Article
- The Msd1-Wdr8-Pkl1 complex anchors microtubule minus ends to fission yeast spindle pole bodies.The Journal of cell biology · 2015Article
- Kinesin-14 and kinesin-5 antagonistically regulate microtubule nucleation by γ-TuRC in yeast and human cells.Nature communications · 2014Article
- Kinesin-14 Pkl1 targets γ-tubulin for release from the γ-tubulin ring complex (γ-TuRC) .Cell cycle (Georgetown, Tex.) · 2013Article
- Coupling of kinesin ATP turnover to translocation and microtubule regulation: one engine, many machines.Journal of muscle research and cell motility · 2012Review
- Tau protein diffuses along the microtubule lattice.The Journal of biological chemistry · 2012Article
- Regulation of mitochondrial transport and inter-microtubule spacing by tau phosphorylation at the sites hyperphosphorylated in Alzheimer's disease.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2012Article
- A single protofilament is sufficient to support unidirectional walking of dynein and kinesin.PloS one · 2012Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Fission yeast Pkl1 is a kinesin-14A family member that is known to be localized at the cellular spindle and is capable of hydrolyzing ATP. However, its motility has not been detected. Here, we show that Pkl1 is a slow, minus end-directed microtubule motor with a maximum velocity of 33+/-9 nm/s. The Km,MT value of steady-state ATPase activity of Pkl1 was as low as 6.4+/-1.1 nM, which is 20-30 times smaller than that of kinesin-1 and another kinesin-14A family member, Ncd, indicating a high affinity of Pkl1 for microtubules. However, the duty ratio of 0.05 indicates that Pkl1 spends only a small fraction of the ATPase cycle strongly associated with a microtubule. By using total internal reflection fluorescence microscopy, we demonstrated that single molecules of Pkl1 were not highly processive but only exhibited biased one-dimensional diffusion along microtubules, whereas several molecules of Pkl1, probably fewer than 10 molecules, cooperatively moved along microtubules and substantially reduced the diffusive component in the movement. Our results suggest that Pkl1 molecules work in groups to move and generate forces in a cooperative manner for their mitotic functions.
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