ArticleProceedings of the National Academy of Sciences of the United States of America2010
A non-ring-like form of the Dam1 complex modulates microtubule dynamics in fission yeast.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 25 citations in OpenAlex.
- Functional plasticity in chromosome-microtubule coupling on the evolutionary time scale.Life science alliance · 2023Article
- Structural view of the yeast Dam1 complex, a ring-shaped molecular coupler for the dynamic microtubule end.Essays in biochemistry · 2020Review
- Mechanisms of chromosome biorientation and bipolar spindle assembly analyzed by computational modeling.eLife · 2020Article
- Ccp1 modulates epigenetic stability at centromeres and affects heterochromatin distribution inThe Journal of biological chemistry · 2018Article
- Structural plasticity of the living kinetochore.The Journal of cell biology · 2017Article
- MAARS: a novel high-content acquisition software for the analysis of mitotic defects in fission yeast.Molecular biology of the cell · 2017Article
- Counting protein molecules using quantitative fluorescence microscopy.Trends in biochemical sciences · 2012Review
- Review
- MoDUO1, a Duo1-like gene, is required for full virulence of the rice blast fungus Magnaporthe oryzae.Current genetics · 2011Article
- CENP-A exceeds microtubule attachment sites in centromere clusters of both budding and fission yeast.The Journal of cell biology · 2011Article
- Growth and shortening of microtubules: a two-state model approach.The Journal of biological chemistry · 2011Article
- The requirement for the Dam1 complex is dependent upon the number of kinetochore proteins and microtubules.Current biology : CB · 2011Article
- Ringing the changes: emerging roles for DASH at the kinetochore-microtubule Interface.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2011Review
- Kinetochores' gripping feat: conformational wave or biased diffusion?Trends in cell biology · 2011Review
- Review
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
The Dam1 complex is a kinetochore component that couples chromosomes to the dynamic ends of kinetochore microtubules (kMTs). Work in the budding yeast Saccharomyces cerevisiae has shown that the Dam1 complex forms a 16-unit ring encircling and tracking the tip of a MT in vitro, consistent with its cellular function as a coupler. Dam1 also forms smaller, nonring patches in vitro that track the dynamic ends of MTs. However, the identity of Dam1's functional form in vivo remains unknown. Here we report a comprehensive in vivo characterization of Dam1 in the fission yeast Schizosaccharomyces pombe. In addition to their dense localizations on kinetochores and spindle MTs during mitosis, we identify that Dam1 is also localized onto cytoplasmic MTs as discrete spots in interphase, providing the unique opportunity to analyze Dam1 oligomers at the single-particle resolution in live cells. Such analysis shows that each oligomer contains one to five copies of Dam1, and is able to "switch-rail" while moving along MTs, precluding the possibility of a 16-unit encircling structure. Dam1 patches track the plus ends of the shortening, but not the elongating, MTs and retard MT depolymerization. Together with Mal3, the EB1-like MT-interacting protein, cytoplasmic Dam1 plays an important role in maintaining proper cell shape. In mitosis, kinetochore-associated Dam1 appears to facilitate kMT depolymerization. Together, our findings suggest that patches, instead of rings, are the physiologically functional forms of Dam1 in pombe. Our findings help establish the benchmark parameters of the Dam1 coupler and elucidate the mechanism of its functions.
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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.