ArticleCurrent biology : CB2015
The Mechanochemical Cycle of Mammalian Kinesin-2 KIF3A/B under Load.
Article in Current biology : CB, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
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Who cites it
56 citing papers in PubMed, 97 citations in OpenAlex.
- Article
- An Overview of Contrasting Experimental Results on Dynamics of Kinesin-1 Molecular Motors: Insight into the Underlying Mechanism.Biomolecules · 2025Review
- Kinesin-1 autoinhibition tunes cargo transport by motor ensembles.Biophysical journal · 2025Article
- Regulation of kinesin-2 motility by its β-hairpin motif.Nature structural & molecular biology · 2025Article
- PRC1 resists microtubule sliding in two distinct resistive modes due to variations in the separation between overlapping microtubules.Molecular biology of the cell · 2025Article
- DNA tensiometer reveals catch-bond detachment kinetics of kinesin-1, -2 and -3.bioRxiv : the preprint server for biology · 2025Article
- A mutual co-recognition mechanism ensures the proper assembly of heterotrimeric kinesin-2 for intraflagellar transport.Nature communications · 2025Article
- PRC1 resists microtubule sliding in two distinct resistive modes due to variations in the separation between overlapping microtubules.bioRxiv : the preprint server for biology · 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
- One must reconstitute the functions of interest from purified proteins.Frontiers in physiology · 2024Review
- Simulations suggest robust microtubule attachment of kinesin and dynein in antagonistic pairs.Biophysical journal · 2023Article
- Determinant factors for residence time of kinesin motors at microtubule ends.Journal of biological physics · 2023Article
- The interplay of active and passive mechanisms in slow axonal transport.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
- KAP is the neuronal organelle adaptor for Kinesin-2 KIF3AB and KIF3AC.Molecular biology of the cell · 2022Article
- Article
- Review
- Directly Measuring Forces within Reconstituted Active Microtubule Bundles.Journal of visualized experiments : JoVE · 2022Article
- Ultrafast Force-Clamp Spectroscopy of Microtubule-Binding Proteins.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Pathogenic mutations in the kinesin-3 motor KIF1A diminish force generation and movement through allosteric mechanisms.The Journal of cell biology · 2021Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The response of motor proteins to external loads underlies their ability to work in teams and determines the net speed and directionality of cargo transport. The mammalian kinesin-2, KIF3A/B, is a heterotrimeric motor involved in intraflagellar transport and vesicle motility in neurons. Bidirectional cargo transport is known to result from the opposing activities of KIF3A/B and dynein bound to the same cargo, but the load-dependent properties of kinesin-2 are poorly understood. We used a feedback-controlled optical trap to probe the velocity, run length, and unbinding kinetics of mouse KIF3A/B under various loads and nucleotide conditions. The kinesin-2 motor velocity is less sensitive than kinesin-1 to external forces, but its processivity diminishes steeply with load, and the motor was observed occasionally to slip and reattach. Each motor domain was characterized by studying homodimeric constructs, and a global fit to the data resulted in a comprehensive pathway that quantifies the principal force-dependent kinetic transitions. The properties of the KIF3A/B heterodimer are intermediate between the two homodimers, and the distinct load-dependent behavior is attributable to the properties of the motor domains and not to the neck linkers or the coiled-coil stalk. We conclude that the force-dependent movement of KIF3A/B differs significantly from conventional kinesin-1. Against opposing dynein forces, KIF3A/B motors are predicted to rapidly unbind and rebind, resulting in qualitatively different transport behavior from kinesin-1.
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Registered trials
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.