ArticleNature communications2017
The mitotic kinesin-14 KlpA contains a context-dependent directionality switch.
Article in Nature communications, 2017. 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.
- Dimeric Cin8 motors have an inherent plus-end bias and weak interhead coordination.Biophysical journal · 2026Article
- Structural analysis of a motor with increased mechanical output reveals new transitions in kinesin microtubule motility.Scientific reports · 2026Article
- Dimeric Cin8 motors have an inherent plus-end bias and weak inter-head coordination.bioRxiv : the preprint server for biology · 2025Article
- Mechanism and regulation of kinesin motors.Nature reviews. Molecular cell biology · 2025Review
- Two Tetrahymena kinesin-9 family members exhibit slow plus-end-directed motility in vitro.Scientific reports · 2024Article
- Kinesin-14 HSET and KlpA are non-processive microtubule motors with load-dependent power strokes.Nature communications · 2024Article
- Modeling Studies of the Mechanism of Context-Dependent Bidirectional Movements of Kinesin-14 Motors.Molecules (Basel, Switzerland) · 2024Article
- Direct observation of coordinated assembly of individual native centromeric nucleosomes.The EMBO journal · 2023Article
- Direct observation of coordinated assembly of individual native centromeric nucleosomes.bioRxiv : the preprint server for biology · 2023Article
- Anchoring geometry is a significant factor in determining the direction of kinesin-14 motility on microtubules.Scientific reports · 2022Article
- Computational Study on E-Hooks of Tubulins in the Binding Process with Kinesin.International journal of molecular sciences · 2022Article
- Flexible microtubule anchoring modulates the bi-directional motility of the kinesin-5 Cin8.Cellular and molecular life sciences : CMLS · 2021Article
- Drag-induced directionality switching of kinesin-5 Cin8 revealed by cluster-motility analysis.Science advances · 2021Article
- The Tail of Kinesin-14a in Giardia Is a Dual Regulator of Motility.Current biology : CB · 2020Article
- Distinct kinesin motors drive two types of maize neocentromeres.Genes & development · 2020Article
- Synthetic biology approaches to dissecting linear motor protein function: towards the design and synthesis of artificial autonomous protein walkers.Biophysical reviews · 2020Review
- De novo Transcriptome of the Non-saxitoxin ProducingMarine drugs · 2020Article
- Directional Stepping Model for Yeast Dynein: Longitudinal- and Side-Step Distributions.Biophysical journal · 2019Article
- The Orphan Kinesin PAKRP2 Achieves Processive Motility via a Noncanonical Stepping Mechanism.Biophysical journal · 2019Article
- Processive Kinesin-14 HSET Exhibits Directional Flexibility Depending on Motor Traffic.Current biology : CB · 2018Article
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Kinesin-14s are commonly known as nonprocessive minus end-directed microtubule motors that function mainly for mitotic spindle assembly. Here we show using total internal reflection fluorescence microscopy that KlpA-a kinesin-14 from Aspergillus nidulans-is a context-dependent bidirectional motor. KlpA exhibits plus end-directed processive motility on single microtubules, but reverts to canonical minus end-directed motility when anchored on the surface in microtubule-gliding experiments or interacting with a pair of microtubules in microtubule-sliding experiments. Plus end-directed processive motility of KlpA on single microtubules depends on its N-terminal nonmotor microtubule-binding tail, as KlpA without the tail is nonprocessive and minus end-directed. We suggest that the tail is a de facto directionality switch for KlpA motility: when the tail binds to the same microtubule as the motor domain, KlpA is a plus end-directed processive motor; in contrast, when the tail detaches from the microtubule to which the motor domain binds, KlpA becomes minus end-directed.
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