ArticleThe Journal of biological chemistry2020
A kinetic dissection of the fast and superprocessive kinesin-3 KIF1A reveals a predominant one-head-bound state during its chemomechanical cycle.
Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Article
- Oxidative stress impairs processive motility of the axonal transport motor KIF1A.The Journal of biological chemistry · 2026Article
- KLP-6 is a kinesin superfamily protein resistant to ADP inhibition.Communications biology · 2026Article
- Dimeric Cin8 motors have an inherent plus-end bias and weak interhead coordination.Biophysical journal · 2026Article
- Dimeric Cin8 motors have an inherent plus-end bias and weak inter-head coordination.bioRxiv : the preprint server for biology · 2025Article
- An Overview of Contrasting Experimental Results on Dynamics of Kinesin-1 Molecular Motors: Insight into the Underlying Mechanism.Biomolecules · 2025Review
- DNA tensiometer reveals catch-bond detachment kinetics of kinesin-1, -2 and -3.bioRxiv : the preprint server for biology · 2025Article
- Factors Determining Kinesin Motors in a Predominant One-Head-Bound or Two-Heads-Bound State During Its Stepping Cycle.Biomolecules · 2025Article
- Dissecting the pH Sensitivity of Kinesin-Driven Transport.The journal of physical chemistry. B · 2024Article
- Cryo-EM unveils kinesin KIF1A's processivity mechanism and the impact of its pathogenic variant P305L.Nature communications · 2024Article
- A Model for Chemomechanical Coupling of Kinesin-3 Motor.Cellular and molecular bioengineering · 2024Article
- Modeling the motion of disease-associated KIF1A heterodimers.Biophysical journal · 2023Article
- KIF1A is kinetically tuned to be a superengaging motor under hindering loads.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Synergy between inhibitors of two mitotic spindle assembly motors undermines an adaptive response.Molecular biology of the cell · 2022Article
- Article
- Force generation of KIF1C is impaired by pathogenic mutations.Current biology : CB · 2022Article
- Kinesin-3 motors are fine-tuned at the molecular level to endow distinct mechanical outputs.BMC biology · 2022Article
- A kinesin-1 variant reveals motor-induced microtubule damage in cells.Current biology : CB · 2022Article
- Optical Control of Mitosis with a Photoswitchable Eg5 Inhibitor.Angewandte Chemie (International ed. in English) · 2022Article
- Cellular functions of actin- and microtubule-associated septins.Current biology : CB · 2021Review
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4 authors.
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Abstract
The kinesin-3 family contains the fastest and most processive motors of the three neuronal transport kinesin families, yet the sequence of states and rates of kinetic transitions that comprise the chemomechanical cycle and give rise to their unique properties are poorly understood. We used stopped-flow fluorescence spectroscopy and single-molecule motility assays to delineate the chemomechanical cycle of the kinesin-3, KIF1A. Our bacterially expressed KIF1A construct, dimerized via a kinesin-1 coiled-coil, exhibits fast velocity and superprocessivity behavior similar to WT KIF1A. We established that the KIF1A forward step is triggered by hydrolysis of ATP and not by ATP binding, meaning that KIF1A follows the same chemomechanical cycle as established for kinesin-1 and -2. The ATP-triggered half-site release rate of KIF1A was similar to the stepping rate, indicating that during stepping, rear-head detachment is an order of magnitude faster than in kinesin-1 and kinesin-2. Thus, KIF1A spends the majority of its hydrolysis cycle in a one-head-bound state. Both the ADP off-rate and the ATP on-rate at physiological ATP concentration were fast, eliminating these steps as possible rate-limiting transitions. Based on the measured run length and the relatively slow off-rate in ADP, we conclude that attachment of the tethered head is the rate-limiting transition in the KIF1A stepping cycle. Thus, KIF1A's activity can be explained by a fast rear-head detachment rate, a rate-limiting step of tethered-head attachment that follows ATP hydrolysis, and a relatively strong electrostatic interaction with the microtubule in the weakly bound post-hydrolysis state.
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