ArticleeLife2018
Multivalency of NDC80 in the outer kinetochore is essential to track shortening microtubules and generate forces.
Article in eLife, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 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
54 citing papers in PubMed, 85 citations in OpenAlex.
- Structure and function of the outer kinetochore.Nature reviews. Molecular cell biology · 2026Review
- Low kinetochore-microtubule occupancy leaves a mitotic memory by delaying checkpoint silencing.Nature communications · 2026Article
- Microtubule-Associated Proteins: From Dynamic Regulation of Microtubules to Cellular Architecture.Cells · 2026Review
- Structural Basis of Human Kinetochore-Microtubule Coupling by the Ndc80 and Ska Complexes.bioRxiv : the preprint server for biology · 2026Article
- Microtubule end stabilisation by cooperative oligomers of Ska and Ndc80 complexes.The EMBO journal · 2026Article
- Microtubules guide Aurora B substrate geometries for accurate chromosome segregation.Science advances · 2026Article
- From Single Ligand-Receptor Bond Strength to Collective Avidity: Mechanics-Guided Superselective Nanoparticle Adhesion to Biological Membranes.Langmuir : the ACS journal of surfaces and colloids · 2025Article
- Mammalian metaphase kinetochores are elastic and require condensin for robust structure and function.bioRxiv : the preprint server for biology · 2025Article
- Microtubule dynamics are defined by conformations and stability of clustered protofilaments.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- SEC-SAXS/MC Ensemble Structural Studies of the Microtubule Binding Protein Cdt1 Show Monomeric, Folded-Over Conformations.Cytoskeleton (Hoboken, N.J.) · 2025Article
- Force-transducing molecular ensembles at growing microtubule tips control mitotic spindle size.Nature communications · 2024Article
- Structure of the human KMN complex and implications for regulation of its assembly.Nature structural & molecular biology · 2024Article
- SAXS/MC studies of the mixed-folded protein Cdt1 reveal monomeric, folded over conformations.bioRxiv : the preprint server for biology · 2024Article
- Higher-order protein assembly controls kinetochore formation.Nature cell biology · 2024Article
- Article
- A general model for the motion of multivalent cargo interacting with substrates.Journal of the Royal Society, Interface · 2023Article
- Mechanical coupling coordinates microtubule growth.bioRxiv : the preprint server for biology · 2023Article
- Measuring and modeling forces generated by microtubules.Biophysical reviews · 2023Review
- Stable kinetochore-microtubule attachment requires loop-dependent Ndc80-Ndc80 binding.The EMBO journal · 2023Article
- Herding of proteins by the ends of shrinking polymers.Physical review. E · 2023Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Presence of multiple copies of the microtubule-binding NDC80 complex is an evolutionary conserved feature of kinetochores, points of attachment of chromosomes to spindle microtubules. This may enable multivalent attachments to microtubules, with implications that remain unexplored. Using recombinant human kinetochore components, we show that while single NDC80 complexes do not track depolymerizing microtubules, reconstituted particles containing the NDC80 receptor CENP-T bound to three or more NDC80 complexes do so effectively, as expected for a kinetochore force coupler. To study multivalency systematically, we engineered modules allowing incremental addition of NDC80 complexes. The modules' residence time on microtubules increased exponentially with the number of NDC80 complexes. Modules with two or more complexes tracked depolymerizing microtubules with increasing efficiencies, and stalled and rescued microtubule depolymerization in a force-dependent manner when conjugated to cargo. Our observations indicate that NDC80, rather than through biased diffusion, tracks depolymerizing microtubules by harnessing force generated during microtubule disassembly.
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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.