ArticleOpen biology2016
Molecular architecture of the Dam1 complex-microtubule interaction.
Article in Open biology, 2016. 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
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
19 citing papers in PubMed, 33 citations in OpenAlex.
- Cell cycle dependent methylation of Dam1 contributes to kinetochore integrity and faithful chromosome segregation.PLoS genetics · 2025Article
- Spindle integrity is regulated by a phospho-dependent interaction between the Ndc80 and Dam1 kinetochore complexes.PLoS genetics · 2025Article
- Structural basis for α-tubulin-specific and modification state-dependent glutamylation.Nature chemical biology · 2024Article
- Structural mechanism of outer kinetochore Dam1-Ndc80 complex assembly on microtubules.Science (New York, N.Y.) · 2023Article
- Functional plasticity in chromosome-microtubule coupling on the evolutionary time scale.Life science alliance · 2023Article
- Structure of the Ndc80 complex and its interactions at the yeast kinetochore-microtubule interface.Open biology · 2023Article
- Article
- A Crosslinking Mass Spectrometry Protocol for the Structural Analysis of Microtubule-Associated Proteins.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Phospho-regulated Bim1/EB1 interactions trigger Dam1c ring assembly at the budding yeast outer kinetochore.The EMBO journal · 2021Article
- Aurora B switches relative strength of kinetochore-microtubule attachment modes for error correction.The Journal of cell biology · 2021Article
- Structural view of the yeast Dam1 complex, a ring-shaped molecular coupler for the dynamic microtubule end.Essays in biochemistry · 2020Review
- Seeing is believing: our evolving view of kinetochore structure, composition, and assembly.Current opinion in cell biology · 2019Review
- Outer kinetochore protein Dam1 promotes centromere clustering in parallel with Slk19 in budding yeast.Chromosoma · 2019Article
- Electron cryotomography analysis of Dam1C/DASH at the kinetochore-spindle interface in situ.The Journal of cell biology · 2019Article
- Glucose Signaling Is Connected to Chromosome Segregation Through Protein Kinase A Phosphorylation of the Dam1 Kinetochore Subunit inGenetics · 2019Article
- Efficient and robust proteome-wide approaches for cross-linking mass spectrometry.Nature protocols · 2018Article
- Structure of the DASH/Dam1 complex shows its role at the yeast kinetochore-microtubule interface.Science (New York, N.Y.) · 2018Article
- Article
- A Molecular View of Kinetochore Assembly and Function.Biology · 2017Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 2 countries.
Funding
Abstract
Mitosis is a highly regulated process that allows the equal distribution of the genetic material to the daughter cells. Chromosome segregation requires the formation of a bipolar mitotic spindle and assembly of a multi-protein structure termed the kinetochore to mediate attachments between condensed chromosomes and spindle microtubules. In budding yeast, a single microtubule attaches to each kinetochore, necessitating robustness and processivity of this kinetochore-microtubule attachment. The yeast kinetochore-localized Dam1 complex forms a direct interaction with the spindle microtubule. In vitro, the Dam1 complex assembles as a ring around microtubules and couples microtubule depolymerization with cargo movement. However, the subunit organization within the Dam1 complex, its higher-order oligomerization and how it interacts with microtubules remain under debate. Here, we used chemical cross-linking and mass spectrometry to define the architecture and subunit organization of the Dam1 complex. This work reveals that both the C termini of Duo1 and Dam1 subunits interact with the microtubule and are critical for microtubule binding of the Dam1 complex, placing Duo1 and Dam1 on the inside of the ring structure. Integrating this information with available structural data, we provide a coherent model for how the Dam1 complex self-assembles around microtubules.
Indexed as
Identifiers
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.