ArticleBiochemical and biophysical research communications2010
Torque generation by one of the motor subunits of heterotrimeric kinesin-2.
Article in Biochemical and biophysical research communications, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Motor generated torque drives coupled yawing and orbital rotations of kinesin coated gold nanorods.Communications biology · 2022Article
- KAP is the neuronal organelle adaptor for Kinesin-2 KIF3AB and KIF3AC.Molecular biology of the cell · 2022Article
- Anchoring geometry is a significant factor in determining the direction of kinesin-14 motility on microtubules.Scientific reports · 2022Article
- Review
- CYK4 relaxes the bias in the off-axis motion by MKLP1 kinesin-6.Communications biology · 2021Article
- Functional exploration of heterotrimeric kinesin-II in IFT and ciliary length control ineLife · 2020Article
- The crowding dynamics of the motor protein kinesin-II.PloS one · 2020Article
- 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
- 3D motion of vesicles along microtubules helps them to circumvent obstacles in cells.Journal of cell science · 2017Article
- Kinesin Motor Enzymology: Chemistry, Structure, and Physics of Nanoscale Molecular Machines.Biophysical reviews · 2015Article
- The Kinesin-8 Kip3 switches protofilaments in a sideward random walk asymmetrically biased by force.Biophysical journal · 2015Article
- The highly processive kinesin-8, Kip3, switches microtubule protofilaments with a bias toward the left.Biophysical journal · 2012Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Heterotrimeric kinesin-2 motors transport intraflagellar transport (IFT)-particles from the base to the tip of the axoneme to assemble and maintain cilia. These motors are distinct in containing two non-identical motor subunits together with an accessory subunit. We evaluated the significance of this organization by comparing purified wild type kinesin-2 holoenzymes that support IFT in vivo, with mutant trimers containing only one type of motor domain that do not support IFT in vivo. In motility assays, wild type kinesin-2 moved microtubules (MTs) at a rate intermediate between the rates supported by the two mutants. Interestingly, one of the mutants, but not the other mutant or the wild type protein, was observed to drive a persistent counter-clock-wise rotation of the gliding MTs. Thus one of the two motor domains of heterotrimeric kinesin-2 exerts torque as well as axial force as it moves along a MT, which may allow kinesin-2 to control its circumferential position around a MT doublet within the cilium.
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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.