ArticleMolecular biology of the cell2011
The Dam1 ring binds to the E-hook of tubulin and diffuses along the microtubule.
Article in Molecular biology of the cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 46 citations in OpenAlex.
- Structural mechanism of outer kinetochore Dam1-Ndc80 complex assembly on microtubules.Science (New York, N.Y.) · 2023Article
- Measuring and modeling forces generated by microtubules.Biophysical reviews · 2023Review
- Structure of the Ndc80 complex and its interactions at the yeast kinetochore-microtubule interface.Open biology · 2023Article
- The Four Causes: The Functional Architecture of Centromeres and Kinetochores.Annual review of genetics · 2022Review
- Phospho-regulated Bim1/EB1 interactions trigger Dam1c ring assembly at the budding yeast outer kinetochore.The EMBO journal · 2021Article
- Cdk1 Phosphorylation of the Dam1 Complex Strengthens Kinetochore-Microtubule Attachments.Current biology : CB · 2020Article
- Structural view of the yeast Dam1 complex, a ring-shaped molecular coupler for the dynamic microtubule end.Essays in biochemistry · 2020Review
- Processivity vs. Beating: Comparing Cytoplasmic and Axonemal Dynein Microtubule Binding Domain Association with Microtubule.International journal of molecular sciences · 2019Article
- Electron cryotomography analysis of Dam1C/DASH at the kinetochore-spindle interface in situ.The Journal of cell biology · 2019Article
- Cdt1 stabilizes kinetochore-microtubule attachments via an Aurora B kinase-dependent mechanism.The Journal of cell biology · 2018Article
- E-hooks provide guidance and a soft landing for the microtubule binding domain of dynein.Scientific reports · 2018Article
- Structure of the DASH/Dam1 complex shows its role at the yeast kinetochore-microtubule interface.Science (New York, N.Y.) · 2018Article
- A Molecular View of Kinetochore Assembly and Function.Biology · 2017Review
- Molecular architecture of the Dam1 complex-microtubule interaction.Open biology · 2016Article
- The molecular architecture of the Dam1 kinetochore complex is defined by cross-linking based structural modelling.Nature communications · 2015Article
- Structural maintenance of chromosome (SMC) proteins link microtubule stability to genome integrity.The Journal of biological chemistry · 2014Article
- The family-specific K-loop influences the microtubule on-rate but not the superprocessivity of kinesin-3 motors.Molecular biology of the cell · 2014Article
- Assembling the protein architecture of the budding yeast kinetochore-microtubule attachment using FRET.Current biology : CB · 2014Article
- An array of nuclear microtubules reorganizes the budding yeast nucleus during quiescence.The Journal of cell biology · 2013Article
- Phosphorylation regulates kinase and microtubule binding activities of the budding yeast chromosomal passenger complex in vitro.The Journal of biological chemistry · 2013Article
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
There has been much effort in recent years aimed at understanding the molecular mechanism by which the Dam1 kinetochore complex is able to couple microtubule depolymerization to poleward movement. Both a biased diffusion and a forced walk model have been proposed, and several key functional aspects of Dam1-microtubule binding are disputed. Here, we investigate the elements involved in tubulin-Dam1 complex interactions and directly visualize Dam1 rings on microtubules in order to infer their dynamic behavior on the microtubule lattice and its likely relevance at the kinetochore. We find that the Dam1 complex has a preference for native tubulin over tubulin that is lacking its acidic C-terminal tail. Statistical mechanical analysis of images of Dam1 rings on microtubules, applied to both the distance between rings and the tilt angle of the rings with respect to the microtubule axis, supports a diffusive ring model. We also present a cryo-EM reconstruction of the Dam1 ring, likely the relevant assembly form of the complex for energy coupling during microtubule depolymerization in budding yeast. The present studies constitute a significant step forward by linking structural and biochemical observations toward a comprehensive understanding of the Dam1 complex.
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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.