ArticleBiophysical journal2020
Backstepping Mechanism of Kinesin-1.
Article in Biophysical journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Enhanced processivity and collective force production of kinesin-1 at low radial forces.eLife · 2026Article
- Article
- Clocked stepping of an artificial protein walker along a DNA track.Nature nanotechnology · 2026Article
- ATPγS substantially defeats the biasing mechanism for kinesin steps.Nature communications · 2026Article
- Enhanced Processivity and Collective Force Production of Kinesin-1 at Low Radial Forces.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
- 'Intelligent' proteins.Cellular and molecular life sciences : CMLS · 2025Review
- Genome-wide identification of the key kinesin genes during fiber and boll development in upland cotton (Gossypium hirsutum L.).Molecular genetics and genomics : MGG · 2024Article
- Genome-wide identification of the key Kinesin genes during fiber and boll development in upland cotton (Gossypium hirsutum L).Molecular genetics and genomics : MGG · 2024Article
- Simulations suggest robust microtubule attachment of kinesin and dynein in antagonistic pairs.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
- Information flow, gating, and energetics in dimeric molecular motors.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Article
- Force generation of KIF1C is impaired by pathogenic mutations.Current biology : CB · 2022Article
- A mechanochemical model of the forward/backward movement of motor protein kinesin-1.The Journal of biological chemistry · 2022Article
- Force and Stepwise Movements of Gliding Motility in Human Pathogenic BacteriumFrontiers in microbiology · 2021Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Kinesin-1 is an ATP-driven molecular motor that transports cellular cargo along microtubules. At low loads, kinesin-1 almost always steps forward, toward microtubule plus ends, but at higher loads, it can also step backward. Backsteps are usually 8 nm but can be larger. These larger backward events of 16 nm, 24 nm, or more are thought to be slips rather than steps because they are too fast to consist of multiple, tightly coupled 8-nm steps. Here, we propose that not only these larger backsteps, but all kinesin-1 backsteps, are slips. We show first that kinesin waits before forward steps for less time than before backsteps and detachments; second, we show that kinesin waits for the same amount of time before backsteps and detachments; and third, we show that by varying the microtubule type, we can change the ratio of backsteps to detachments without affecting forward stepping. Our findings indicate that backsteps and detachments originate from the same state and that this state arises later in the mechanochemical cycle than the state that gives rise to forward steps. To explain our data, we propose that, in each cycle of ATP turnover, forward kinesin steps can only occur before Pi release, whereas backslips and detachments can only occur after Pi release. In the scheme we propose, Pi release gates access to a weak binding K⋅ADP-K⋅ADP state that can slip back along the microtubule, re-engage, release ADP, and try again to take an ATP-driven forward step. We predict that this rescued detachment pathway is key to maintaining kinesin processivity under load.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.