ArticleNature structural & molecular biology2013
Structure of a kinesin-tubulin complex and implications for kinesin motility.
Article in Nature structural & molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 104 papers.
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Who cites it
104 citing papers in PubMed, 168 citations in OpenAlex.
- Anisotropic unbinding and location-dependent hovering of a kinesin motor head over microtubule.Biophysical journal · 2026Article
- Neck region-microtubule interactions direct counterclockwise stepping of kinesin-1.Biophysical journal · 2026Article
- 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
- Regulation of kinesin-2 motility by its β-hairpin motif.Nature structural & molecular biology · 2025Article
- Time-Resolved Crystallography Reveals the Mechanisms of GTP hydrolysis for N-RAS and the Oncogenic Mutants G12C, G12V and Q61L.bioRxiv : the preprint server for biology · 2025Article
- Tension-induced suppression of allosteric conformational changes coordinates kinesin-1 stepping.The Journal of cell biology · 2025Article
- Microtubule association induces a Mg-free apo-like ADP pre-release conformation in kinesin-1 that is unaffected by its autoinhibitory tail.Nature communications · 2025Article
- Kinetic regulation of kinesin's two motor domains coordinates its stepping along microtubules.eLife · 2025Article
- Organometallic Chemistry Tools for Building Biologically Relevant Nanoscale Systems.Journal of the American Chemical Society · 2024Review
- Tubulin CFEOM mutations both inhibit or activate kinesin motor activity.Molecular biology of the cell · 2024Article
- Characterization of the disease-causing mechanism of KIF3B mutations from ciliopathy patients.Frontiers in molecular biosciences · 2024Article
- Structural insights into the mechanism of GTP initiation of microtubule assembly.Nature communications · 2023Article
- Nucleotide-free structures of KIF20A illuminate atypical mechanochemistry in this kinesin-6.Open biology · 2023Article
- The motor domain of the kinesin Kip2 promotes microtubule polymerization at microtubule tips.The Journal of cell biology · 2023Article
- The distinct initiation sites and processing activities of TTLL4 and TTLL7 in glutamylation of brain tubulin.The Journal of biological chemistry · 2023Article
- Tubulin polyglutamylation differentially regulates microtubule-interacting proteins.The EMBO journal · 2023Article
- Road-blocker HSP disease mutation disrupts pre-organization for ATP hydrolysis in kinesin through a second sphere control.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Magic-angle-spinning NMR structure of the kinesin-1 motor domain assembled with microtubules reveals the elusive neck linker orientation.Nature communications · 2022Article
- Cytoskeletal and Cytoskeleton-Associated Proteins: Key Regulators of Cancer Stem Cell Properties.Pharmaceuticals (Basel, Switzerland) · 2022Review
44 more citing papers are in PubMed but not listed here.
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Authors and funding
8 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The typical function of kinesins is to transport cargo along microtubules. Binding of ATP to microtubule-attached motile kinesins leads to cargo displacement. To better understand the nature of the conformational changes that lead to the power stroke that moves a kinesin's load along a microtubule, we determined the X-ray structure of human kinesin-1 bound to αβ-tubulin. The structure defines the mechanism of microtubule-stimulated ATP hydrolysis, which releases the kinesin motor domain from microtubules. It also reveals the structural linkages that connect the ATP nucleotide to the kinesin neck linker, a 15-amino acid segment C terminal to the catalytic core of the motor domain, to result in the power stroke. ATP binding to the microtubule-bound kinesin favors neck-linker docking. This biases the attachment of kinesin's second head in the direction of the movement, thus initiating each of the steps taken.
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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.