ArticleProceedings of the National Academy of Sciences of the United States of America2007
In search of an optimal ring to couple microtubule depolymerization to processive chromosome motions.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 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.
The trial behind it
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
53 citing papers in PubMed, 77 citations in OpenAlex.
- Structure and function of the outer kinetochore.Nature reviews. Molecular cell biology · 2026Review
- Ndc80 complex, a conserved coupler for kinetochore-microtubule motility, is a sliding molecular clutch.Science advances · 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
- Cell cycle dependent methylation of Dam1 contributes to kinetochore integrity and faithful chromosome segregation.PLoS genetics · 2025Article
- Measuring and modeling forces generated by microtubules.Biophysical reviews · 2023Review
- Ultrafast Force-Clamp Spectroscopy of Microtubule-Binding Proteins.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Structural view of the yeast Dam1 complex, a ring-shaped molecular coupler for the dynamic microtubule end.Essays in biochemistry · 2020Review
- Mechanisms of microtubule dynamics and force generation examined with computational modeling and electron cryotomography.Nature communications · 2020Article
- Electron cryotomography analysis of Dam1C/DASH at the kinetochore-spindle interface in situ.The Journal of cell biology · 2019Article
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- How Kinetochore Architecture Shapes the Mechanisms of Its Function.Current biology : CB · 2017Review
- Article
- Review
- Electrostatic forces drive poleward chromosome motions at kinetochores.Cell division · 2016Article
- Molecular and Mechanical Causes of Microtubule Catastrophe and Aging.Biophysical journal · 2015Article
- Tubulin bond energies and microtubule biomechanics determined from nanoindentation in silico.Journal of the American Chemical Society · 2014Article
- Kinetochores require oligomerization of Dam1 complex to maintain microtubule attachments against tension and promote biorientation.Nature communications · 2014Article
- Conformational mechanism for the stability of microtubule-kinetochore attachments.Biophysical journal · 2014Article
- Assembling the protein architecture of the budding yeast kinetochore-microtubule attachment using FRET.Current biology : CB · 2014Article
- Accurate phosphoregulation of kinetochore-microtubule affinity requires unconstrained molecular interactions.The Journal of cell biology · 2014Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
Abstract
Mitotic chromosome motions are driven by microtubules (MTs) and associated proteins that couple kinetochores to MT ends. A good coupler should ensure a high stability of attachment, even when the chromosome changes direction or experiences a large opposing force. The optimal coupler is also expected to be efficient in converting the energy of MT depolymerization into chromosome motility. As was shown years ago, a "sleeve"-based, chromosome-associated structure could, in principle, couple MT dynamics to chromosome motion. A recently identified kinetochore complex from yeast, the "Dam1" or "DASH" complex, may function as an encircling coupler in vivo. Some features of the Dam1 ring differ from those of the "sleeve," but whether these differences are significant has not been examined. Here, we analyze theoretically the biomechanical properties of encircling couplers that have properties of the Dam1/DASH complex, such as its large diameter and inward-directed extensions. We demonstrate that, if the coupler is modeled as a wide ring with links that bind the MT wall, its optimal performance is achieved when the linkers are flexible and their binding to tubulin dimers is strong. The diffusive movement of such a coupler is limited, but MT depolymerization can drive its motion via a "forced walk," whose features differ significantly from those of the mechanisms based on biased diffusion. Our analysis identifies key experimental parameters whose values should determine whether the Dam1/DASH ring moves via diffusion or a forced walk.
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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.