ArticleTraffic (Copenhagen, Denmark)2017
The axonal transport motor kinesin-2 navigates microtubule obstacles via protofilament switching.
Article in Traffic (Copenhagen, Denmark), 2017. 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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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
21 citing papers in PubMed, 38 citations in OpenAlex.
- Article
- 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
- Unraveling the interplay of kinesin-1, tau, and microtubules in neurodegeneration associated with Alzheimer's disease.Frontiers in cellular neuroscience · 2024Review
- Characterization of the disease-causing mechanism of KIF3B mutations from ciliopathy patients.Frontiers in molecular biosciences · 2024Article
- Tau, microtubule dynamics, and axonal transport: New paradigms for neurodegenerative disease.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023Article
- Tau differentially regulates the transport of early endosomes and lysosomes.Molecular biology of the cell · 2022Article
- Article
- Tau interferes with axonal neurite stabilization and cytoskeletal composition independently of its ability to associate with microtubules.Biology open · 2020Article
- The ability of the kinesin-2 heterodimer KIF3AC to navigate microtubule networks is provided by the KIF3A motor domain.The Journal of biological chemistry · 2019Article
- Insights into Kinesin-1 Stepping from Simulations and Tracking of Gold Nanoparticle-Labeled Motors.Biophysical journal · 2019Article
- A Brownian Ratchet Model Explains the Biased Sidestepping of Single-Headed Kinesin-3 KIF1A.Biophysical journal · 2019Article
- Polyglutamylation of tubulin's C-terminal tail controls pausing and motility of kinesin-3 family member KIF1A.The Journal of biological chemistry · 2019Article
- The Orphan Kinesin PAKRP2 Achieves Processive Motility via a Noncanonical Stepping Mechanism.Biophysical journal · 2019Article
- KIF18A's neck linker permits navigation of microtubule-bound obstacles within the mitotic spindle.Life science alliance · 2019Article
- Crowd Control: Effects of Physical Crowding on Cargo Movement in Healthy and Diseased Neurons.Frontiers in cellular neuroscience · 2019Review
- Directionally biased sidestepping of Kip3/kinesin-8 is regulated by ATP waiting time and motor-microtubule interaction strength.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Tau directs intracellular trafficking by regulating the forces exerted by kinesin and dynein teams.Traffic (Copenhagen, Denmark) · 2018Article
- Motor Reattachment Kinetics Play a Dominant Role in Multimotor-Driven Cargo Transport.Biophysical journal · 2018Article
- Neurosteroids and oxysterols as potential therapeutic agents for glaucoma and Alzheimer's disease.Neuropsychiatry · 2018Article
- Kinesin-2 motors adapt their stepping behavior for processive transport on axonemes and microtubules.EMBO reports · 2017Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Axonal transport involves kinesin motors trafficking cargo along microtubules that are rich in microtubule-associated proteins (MAPs). Much attention has focused on the behavior of kinesin-1 in the presence of MAPs, which has overshadowed understanding the contribution of other kinesins such as kinesin-2 in axonal transport. We have previously shown that, unlike kinesin-1, kinesin-2 in vitro motility is insensitive to the neuronal MAP Tau. However, the mechanism by which kinesin-2 efficiently navigates Tau on the microtubule surface is unknown. We hypothesized that mammalian kinesin-2 side-steps to adjacent protofilaments to maneuver around MAPs. To test this, we used single-molecule imaging to track the characteristic run length and protofilament switching behavior of kinesin-1 and kinesin-2 motors in the absence and presence of 2 different microtubule obstacles. Under all conditions tested, kinesin-2 switched protofilaments more frequently than kinesin-1. Using computational modeling that recapitulates run length and switching frequencies in the presence of varying roadblock densities, we conclude that kinesin-2 switches protofilaments to navigate around microtubule obstacles. Elucidating the kinesin-2 mechanism of navigation on the crowded microtubule surface provides a refined view of its contribution in facilitating axonal transport.
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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.