ArticleThe EMBO journal2006
High-resolution cryo-EM maps show the nucleotide binding pocket of KIF1A in open and closed conformations.
Article in The EMBO journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers, 1 of them a synthesis that pooled it.
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Who cites it
66 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Monoallelic KIF1A-related disorders: a multicenter cross sectional study and systematic literature review.Journal of neurology · 2022Pooled it
- Structural analysis of a motor with increased mechanical output reveals new transitions in kinesin microtubule motility.Scientific reports · 2026Article
- An Overview of Contrasting Experimental Results on Dynamics of Kinesin-1 Molecular Motors: Insight into the Underlying Mechanism.Biomolecules · 2025Review
- Biased movement of monomeric kinesin-3 KLP-6 explained by a symmetric Brownian ratchet model.Biophysical journal · 2025Article
- Cryo-EM unveils kinesin KIF1A's processivity mechanism and the impact of its pathogenic variant P305L.Nature communications · 2024Article
- CAMSAPs and nucleation-promoting factors control microtubule release from γ-TuRC.Nature cell biology · 2024Article
- New insights into the mechanochemical coupling mechanism of kinesin-microtubule complexes from their high-resolution structures.Biochemical Society transactions · 2023Review
- TUBB3 and KIF21A in neurodevelopment and disease.Frontiers in neuroscience · 2023Review
- Motor generated torque drives coupled yawing and orbital rotations of kinesin coated gold nanorods.Communications biology · 2022Article
- De novo mutations in KIF1A-associated neuronal disorder (KAND) dominant-negatively inhibit motor activity and axonal transport of synaptic vesicle precursors.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Kinesin-8-specific loop-2 controls the dual activities of the motor domain according to tubulin protofilament shape.Nature communications · 2022Article
- Plus and minus ends of microtubules respond asymmetrically to kinesin binding by a long-range directionally driven allosteric mechanism.Science advances · 2022Article
- Mutation of the H12-helix of α-tubulin/MEC-12 disrupts the localization of neuronal mitochondria.microPublication biology · 2022Article
- Cryo-EM structure of a microtubule-bound parasite kinesin motor and implications for its mechanism and inhibition.The Journal of biological chemistry · 2021Article
- Structural basis of mechano-chemical coupling by the mitotic kinesin KIF14.Nature communications · 2021Article
- Genotype and defects in microtubule-based motility correlate with clinical severity inHGG advances · 2021Article
- Biased Brownian Motion of KIF1A and the Role of Tubulin's C-Terminal Tail Studied by Molecular Dynamics Simulation.International journal of molecular sciences · 2021Article
- A kinetic dissection of the fast and superprocessive kinesin-3 KIF1A reveals a predominant one-head-bound state during its chemomechanical cycle.The Journal of biological chemistry · 2020Article
- Expansion of the phenotypic spectrum of de novo missense variants in kinesin family member 1A (KIF1A).Human mutation · 2020Article
- 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
6 more citing papers are in PubMed but not listed here.
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Kinesin is an ATP-driven microtubule (MT)-based motor fundamental to organelle transport. Although a number of kinesin crystal structures have been solved, the structural evidence for coupling between the bound nucleotide and the conformation of kinesin is elusive. In addition, the structural basis of the MT-induced ATPase activity of kinesin is not clear because of the absence of the MT in the structure. Here, we report cryo-electron microscopy structures of the monomeric kinesin KIF1A-MT complex in two nucleotide states at about 10 A resolution, sufficient to reveal the secondary structure. These high-resolution maps visualized clear structural changes that suggest a mechanical pathway from the nucleotide to the neck linker via the motor core rotation. In addition, new nucleotide binding pocket conformations are observed that are different from X-ray crystallographic structures; it is closed in the 5'-adenylyl-imidodiphosphate state, but open in the ADP state. These results suggest a structural model of biased diffusion movement of monomeric kinesin motor.
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