ArticleThe EMBO journal2015
X-ray and Cryo-EM structures reveal mutual conformational changes of Kinesin and GTP-state microtubules upon binding.
Article in The EMBO journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed, 94 citations in OpenAlex.
- Molecular Dynamics Simulations Provide Further Insights into the Allosteric Regulation of the Kinesin-5 Motor Domain by Loop 5.Journal of chemical information and modeling · 2026Article
- An Overview of Contrasting Experimental Results on Dynamics of Kinesin-1 Molecular Motors: Insight into the Underlying Mechanism.Biomolecules · 2025Review
- Tension-induced suppression of allosteric conformational changes coordinates kinesin-1 stepping.The Journal of cell biology · 2025Article
- Modeling study of kinesin-13 MCAK microtubule depolymerase.European biophysics journal : EBJ · 2024Article
- Tether-scanning the kinesin motor domain reveals a core mechanical action.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Modeling Studies of the Mechanism of Context-Dependent Bidirectional Movements of Kinesin-14 Motors.Molecules (Basel, Switzerland) · 2024Article
- New insights into the mechanochemical coupling mechanism of kinesin-microtubule complexes from their high-resolution structures.Biochemical Society transactions · 2023Review
- A Frame-by-Frame Glance at Membrane Fusion Mechanisms: From Viral Infections to Fertilization.Biomolecules · 2023Review
- Preference of CAMSAP3 for expanded microtubule lattice contributes to stabilization of the minus end.Life science alliance · 2023Article
- Magic-angle-spinning NMR structure of the kinesin-1 motor domain assembled with microtubules reveals the elusive neck linker orientation.Nature communications · 2022Article
- Multiple roles for the cytoskeleton in ALS.Experimental neurology · 2022Review
- A kinesin-1 variant reveals motor-induced microtubule damage in cells.Current biology : CB · 2022Article
- A neuropathy-associated kinesin KIF1A mutation hyper-stabilizes the motor-neck interaction during the ATPase cycle.The EMBO journal · 2022Article
- The molecular biology of tubulinopathies: Understanding the impact of variants on tubulin structure and microtubule regulation.Frontiers in cellular neuroscience · 2022Review
- Phosphoregulation of Kinesins Involved in Long-Range Intracellular Transport.Frontiers in cell and developmental biology · 2022Review
- Modeling processive motion of kinesin-13 MCAK and kinesin-14 Cik1-Kar3 molecular motors.Protein science : a publication of the Protein Society · 2021Article
- Studies of Conformational Changes of Tubulin Induced by Interaction with Kinesin Using Atomistic Molecular Dynamics Simulations.International journal of molecular sciences · 2021Article
- A model of processive walking and slipping of kinesin-8 molecular motors.Scientific reports · 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
- Theoretical Analysis of Dynamics of Kinesin Molecular Motors.ACS omega · 2020Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The molecular motor kinesin moves along microtubules using energy from ATP hydrolysis in an initial step coupled with ADP release. In neurons, kinesin-1/KIF5C preferentially binds to the GTP-state microtubules over GDP-state microtubules to selectively enter an axon among many processes; however, because the atomic structure of nucleotide-free KIF5C is unavailable, its molecular mechanism remains unresolved. Here, the crystal structure of nucleotide-free KIF5C and the cryo-electron microscopic structure of nucleotide-free KIF5C complexed with the GTP-state microtubule are presented. The structures illustrate mutual conformational changes induced by interaction between the GTP-state microtubule and KIF5C. KIF5C acquires the 'rigor conformation', where mobile switches I and II are stabilized through L11 and the initial portion of the neck-linker, facilitating effective ADP release and the weak-to-strong transition of KIF5C microtubule affinity. Conformational changes to tubulin strengthen the longitudinal contacts of the GTP-state microtubule in a similar manner to GDP-taxol microtubules. These results and functional analyses provide the molecular mechanism of the preferential binding of KIF5C to GTP-state microtubules.
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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.