ArticleProceedings of the National Academy of Sciences of the United States of America2009
A mobile kinesin-head intermediate during the ATP-waiting state.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 68 citations in OpenAlex.
- Tension-induced suppression of allosteric conformational changes coordinates kinesin-1 stepping.The Journal of cell biology · 2025Article
- Mechanism and regulation of kinesin motors.Nature reviews. Molecular cell biology · 2025Review
- New insights into the mechanochemical coupling mechanism of kinesin-microtubule complexes from their high-resolution structures.Biochemical Society transactions · 2023Review
- Mud binds the kinesin-14 Ncd inBiochemistry and biophysics reports · 2021Article
- Structural basis of mechano-chemical coupling by the mitotic kinesin KIF14.Nature communications · 2021Article
- How Kinesin-1 Utilize the Energy of Nucleotide: The Conformational Changes and Mechanochemical Coupling in the Unidirectional Motion of Kinesin-1.International journal of molecular sciences · 2020Review
- A bio-pen for direct writing of single molecules on user-functionalized surfaces.Nanoscale advances · 2020Article
- How kinesin waits for ATP affects the nucleotide and load dependence of the stepping kinetics.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Shaft Function of Kinesin-1's α4 Helix in the Processive Movement.Cellular and molecular bioengineering · 2019Article
- Insights into Kinesin-1 Stepping from Simulations and Tracking of Gold Nanoparticle-Labeled Motors.Biophysical journal · 2019Article
- 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
- Processivity of dimeric kinesin-1 molecular motors.FEBS open bio · 2018Article
- Fluorescence microscopy applied to intracellular transport by microtubule motors.Journal of biosciences · 2018Review
- KIF15 nanomechanics and kinesin inhibitors, with implications for cancer chemotherapeutics.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Kinesin-2 motors: Kinetics and biophysics.The Journal of biological chemistry · 2018Review
- Use of Single Molecule Fluorescence Polarization Microscopy to Study Protein Conformation and Dynamics of Kinesin-Microtubule Complexes.Methods in molecular biology (Clifton, N.J.) · 2018Article
- Parsing the roles of neck-linker docking and tethered head diffusion in the stepping dynamics of kinesin.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Intraflagellar transport velocity is governed by the number of active KIF17 and KIF3AB motors and their motility properties under load.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Anchor Effect of Interactions Between Kinesin's Nucleotide-Binding Pocket and Microtubule.Cellular and molecular bioengineering · 2017Article
- Distinct Interaction Modes of the Kinesin-13 Motor Domain with the Microtubule.Biophysical journal · 2016Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Kinesin1 is a motor protein that uses the energy from ATP hydrolysis to move intracellular cargoes along microtubules. It contains 2 identical motor domains, or heads, that coordinate their mechano-chemical cycles to move processively along microtubules. The molecular mechanism of coordination between head domains remains unclear, partly because of the lack of structural information on critical intermediates of the kinesin1 mechano-chemical cycle. A point of controversy has been whether before ATP binding, in the so called ATP-waiting state, 1 or 2 motor domains are bound to the microtubule. To address this issue, here we use ensemble and single molecule fluorescence polarization microscopy (FPM) to determine the mobility and orientation of the kinesin1 heads at different ATP concentrations and in heterodimeric constructs with microtubule binding impaired in 1 head. We found evidence for a mobile head during the ATP-waiting state. We incorporate our results into a model for kinesin translocation that accounts well for many reported experimental results.
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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.