ArticleeLife2020
The mechanism of kinesin inhibition by kinesin-binding protein.
Article in eLife, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
19 citing papers in PubMed, 26 citations in OpenAlex.
- A systems-level proteomic analysis identifies kinesin targets of KIFBP during neuronal development.bioRxiv : the preprint server for biology · 2026Article
- KIF15 (Kinesin-12): molecular biology, physiological functions, and roles in disease.Journal of cancer research and clinical oncology · 2026Review
- Rules of the road: how to turn off kinesin motors.The Biochemical journal · 2026Review
- Joubert syndrome 26 protein enforces compartmentalized motility of a ciliary kinesin.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Mechanism and regulation of kinesin motors.Nature reviews. Molecular cell biology · 2025Review
- Maternal genetic variants in kinesin motor domains prematurely increase egg aneuploidy.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Presynaptic perspective: Axonal transport defects in neurodevelopmental disorders.The Journal of cell biology · 2024Review
- Identification of the KIF18A alpha-4 helix as a therapeutic target for chromosomally unstable tumor cells.Frontiers in molecular biosciences · 2024Article
- Modification of the neck-linker of KIF18A alters Microtubule subpopulation preference.Molecular biology of the cell · 2024Article
- Identification of the KIF18A alpha-4 helix as a therapeutic target for chromosomally unstable tumor cells.bioRxiv : the preprint server for biology · 2023Article
- New insights into the mechanochemical coupling mechanism of kinesin-microtubule complexes from their high-resolution structures.Biochemical Society transactions · 2023Review
- MAPping tubulin mutations.Frontiers in cell and developmental biology · 2023Review
- Selective motor activation in organelle transport along axons.Nature reviews. Molecular cell biology · 2022Review
- Selective axonal transport through branch junctions is directed by growth cone signaling and mediated by KIF1/kinesin-3 motors.Cell reports · 2022Article
- Using a comprehensive approach to investigate the interaction between Kinesin-5/Eg5 and the microtubule.Computational and structural biotechnology journal · 2022Article
- Kinesin-binding protein remodels the kinesin motor to prevent microtubule binding.Science advances · 2021Article
- Cryo-EM of kinesin-binding protein: challenges and opportunities from protein-surface interactions.Acta crystallographica. Section D, Structural biology · 2021Article
- Motor proteins at the mitochondria-cytoskeleton interface.Journal of cell science · 2021Review
- Article
Corrections and comments
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Authors and funding
9 authors at 8 institutions in 4 countries.
Funding
Abstract
Subcellular compartmentalisation is necessary for eukaryotic cell function. Spatial and temporal regulation of kinesin activity is essential for building these local environments via control of intracellular cargo distribution. Kinesin-binding protein (KBP) interacts with a subset of kinesins via their motor domains, inhibits their microtubule (MT) attachment, and blocks their cellular function. However, its mechanisms of inhibition and selectivity have been unclear. Here we use cryo-electron microscopy to reveal the structure of KBP and of a KBP-kinesin motor domain complex. KBP is a tetratricopeptide repeat-containing, right-handed α-solenoid that sequesters the kinesin motor domain's tubulin-binding surface, structurally distorting the motor domain and sterically blocking its MT attachment. KBP uses its α-solenoid concave face and edge loops to bind the kinesin motor domain, and selected structure-guided mutations disrupt KBP inhibition of kinesin transport in cells. The KBP-interacting motor domain surface contains motifs exclusively conserved in KBP-interacting kinesins, suggesting a basis for kinesin selectivity.
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What OpenQuestion holds
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.