ArticleBiochemistry2008
Processive movement by a kinesin heterodimer with an inactivating mutation in one head.
Article in Biochemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 27 citations in OpenAlex.
- The kinesin-4 protein KIF27 forms a cytoskeletal scaffold at the transition zone to promote motile cilia structural integrity.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Biased movement of monomeric kinesin-3 KLP-6 explained by a symmetric Brownian ratchet model.Biophysical journal · 2025Article
- Modeling the motion of disease-associated KIF1A heterodimers.Biophysical journal · 2023Article
- Modeling spatiotemporally varying protein-protein interactions in CyLaKS, the Cytoskeleton Lattice-based Kinetic Simulator.The European physical journal. E, Soft matter · 2021Article
- Resolving kinesin stepping: one head at a time.Life science alliance · 2019Article
- Autoinhibition of kinesin-1 is essential to the dendrite-specific localization of Golgi outposts.The Journal of cell biology · 2018Article
- Allosteric conformational change cascade in cytoplasmic dynein revealed by structure-based molecular simulations.PLoS computational biology · 2017Article
- Article
- How Dynein Moves Along Microtubules.Trends in biochemical sciences · 2016Review
- Kinesin Motor Enzymology: Chemistry, Structure, and Physics of Nanoscale Molecular Machines.Biophysical reviews · 2015Article
- Article
- Tension on the linker gates the ATP-dependent release of dynein from microtubules.Nature communications · 2014Article
- Kar3Vik1 mechanochemistry is inhibited by mutation or deletion of the C terminus of the Vik1 subunit.The Journal of biological chemistry · 2013Article
- Modular aspects of kinesin force generation machinery.Biophysical journal · 2013Article
- Article
- Interactions between subunits in heterodimeric Ncd molecules.The Journal of biological chemistry · 2009Article
- Mechanism of cooperative behaviour in systems of slow and fast molecular motors.Physical chemistry chemical physics : PCCP · 2009Article
- Walking the walk: how kinesin and dynein coordinate their steps.Current opinion in cell biology · 2009Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
A single molecule of the motor enzyme kinesin-1 keeps a tight grip on its microtubule track, making tens or hundreds of discrete, unidirectional 8 nm steps before dissociating. This high duty ratio processive movement is thought to require a mechanism in which alternating stepping of the two head domains of the kinesin dimer is driven by alternating, overlapped cycles of ATP hydrolysis by the two heads. The R210K point mutation in Drosophila kinesin heavy chain was reported to disrupt the ability of the enzyme active site to catalyze ATP P-O bond cleavage. We expressed R210K homodimers as well as isolated R210K heads and confirmed that both are essentially inactive. We then coexpressed tagged R210K subunits with untagged wild-type subunits and affinity purified R210K/wild-type heterodimers together with the inactive R210K homodimers. In contrast to the R210K head or homodimer, the heterodimer was a highly active (>50% of wild-type) microtubule-stimulated ATPase, and the heterodimer displayed high duty ratio processive movement in single-molecule motility experiments. Thus, dimerization of a subunit containing the inactivating mutation with a functional subunit can complement the mutation; this must occur either by lowering or by bypassing kinetic barriers in the ATPase or mechanical cycles of the mutant head. The observations provide support for kinesin-1 gating mechanisms in which one head stimulates the rate of essential processes in the other.
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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.