ArticleThe Journal of biological chemistry2014
Stu2, the budding yeast XMAP215/Dis1 homolog, promotes assembly of yeast microtubules by increasing growth rate and decreasing catastrophe frequency.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 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
39 citing papers in PubMed, 60 citations in OpenAlex.
- Article
- Stu2 performs an essential kinetochore function independent of its microtubule polymerase activity.The Journal of cell biology · 2025Article
- Structural insights into the interplay between microtubule polymerases, γ-tubulin complexes and their receptors.Nature communications · 2025Article
- Dynamic microtubules slow down during their shrinkage phase.Biophysical journal · 2023Article
- Fission yeast Dis1 is an unconventional TOG/XMAP215 that induces microtubule catastrophe to drive chromosome pulling.Communications biology · 2022Article
- The TOG protein Stu2 is regulated by acetylation.PLoS genetics · 2022Article
- Reconstituting Microtubules: A Decades-Long Effort From Building Block Identification to the Generation of Recombinant α/β-Tubulin.Frontiers in cell and developmental biology · 2022Review
- Slk19 enhances cross-linking of microtubules by Ase1 and Stu1.Molecular biology of the cell · 2021Article
- Kinesin-6 Klp9 orchestrates spindle elongation by regulating microtubule sliding and growth.eLife · 2021Article
- Mps1 promotes poleward chromosome movements in meiotic prometaphase.Molecular biology of the cell · 2021Article
- Impact of the 'tubulin economy' on the formation and function of the microtubule cytoskeleton.Current opinion in cell biology · 2021Review
- Microtubule polymerase and processive plus-end tracking functions originate from distinct features within TOG domain arrays.Molecular biology of the cell · 2019Article
- Mapping the kinetochore MAP functions required for stabilizing microtubule attachments to chromosomes during metaphase.Cytoskeleton (Hoboken, N.J.) · 2019Review
- Rescuing microtubules from the brink of catastrophe: CLASPs lead the way.Current opinion in cell biology · 2019Review
- Microtubule dynamics regulation reconstituted in budding yeast lysates.Journal of cell science · 2018Article
- Article
- The TOG protein Stu2/XMAP215 interacts covalently and noncovalently with SUMO.Cytoskeleton (Hoboken, N.J.) · 2018Article
- Microtubule dynamics: an interplay of biochemistry and mechanics.Nature reviews. Molecular cell biology · 2018Review
- Design principles of a microtubule polymerase.eLife · 2018Article
- Human CLASP2 specifically regulates microtubule catastrophe and rescue.Molecular biology of the cell · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Stu2 is the budding yeast member of the XMAP215/Dis1 family of microtubule polymerases. It is essential in cell division, allowing proper spindle orientation and metaphase chromosome alignment, as well as spindle elongation during anaphase. Despite Stu2 having a phenotype that suggests it promotes microtubule growth, like the other members of the XMAP215/Dis1 family, previous studies with purified Stu2 indicate only that it antagonizes microtubule growth. One potential explanation for these contradictory findings is that the assays were performed with mammalian brain tubulin, which may not be the right substrate to test the activity of Stu2 given that yeast and brain tubulins are quite divergent in sequence and that the vertebrate tubulins are subject to many post-translational modifications. To test this possibility, we reconstituted the activity of Stu2 with purified budding yeast tubulin. We found that Stu2 accelerated microtubule growth in yeast tubulin by severalfold, similar to the acceleration reported for XMAP215 in porcine brain tubulin. Furthermore, Stu2 accelerated polymerization in yeast tubulin to a much greater extent than in porcine brain tubulin, and the concentration of Stu2 required to reach 50% maximum activity in yeast tubulin was nearly 2 orders of magnitude lower than that in porcine brain tubulin. We conclude that Stu2 is a microtubule polymerase, like its relatives, and that its activity is considerably higher in yeast tubulin compared with mammalian brain tubulin. The biochemical properties of Stu2 reported here account for many of the phenotypes of Stu2 observed in cells.
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.