ArticleMolecular biology of the cell2018
Stu2 acts as a microtubule destabilizer in metaphase budding yeast spindles.
Article in Molecular biology of the cell, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 20 citations in OpenAlex.
- Stu2 performs an essential kinetochore function independent of its microtubule polymerase activity.The Journal of cell biology · 2025Article
- A coordinated kinase and phosphatase network regulates Stu2 recruitment to yeast kinetochores.The Journal of cell biology · 2025Article
- Evolutionary adaptation to hyperstable microtubules selectively targets tubulins and is empowered by the spindle assembly checkpoint.Cell reports · 2025Article
- The doublecortin-family kinase ZYG-8DCLK1 regulates microtubule dynamics and motor-driven forces to promote the stability of C. elegans acentrosomal spindles.PLoS genetics · 2024Article
- Robust microtubule dynamics facilitate low-tension kinetochore detachment in metaphase.The Journal of cell biology · 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
- Mps1 promotes poleward chromosome movements in meiotic prometaphase.Molecular biology of the cell · 2021Article
- Article
- Kinetochore-associated Stu2 promotes chromosome biorientation in vivo.PLoS genetics · 2019Article
- XMAP215 promotes microtubule-F-actin interactions to regulate growth cone microtubules during axon guidance inJournal of cell science · 2019Article
- The TOG protein Stu2/XMAP215 interacts covalently and noncovalently with SUMO.Cytoskeleton (Hoboken, N.J.) · 2018Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The microtubule-associated protein Stu2 (XMAP215) has the remarkable ability to act either as a polymerase or as a destabilizer of the microtubule plus end. In budding yeast, it is required for the dynamicity of spindle microtubules and also for kinetochore force generation. To understand how Stu2 contributes to these distinct activities, we analyzed the contributions of its functional domains to its localization and function. We find that Stu2 colocalizes with kinetochores using its TOG domains, which bind GTP-tubulin, a coiled-coil homodimerization domain, and a domain that interacts with plus-end interacting proteins. Stu2 localization is also promoted by phosphorylation at a putative CDK1 phosphorylation site located within its microtubule-binding basic patch. Surprisingly, however, we find that kinetochore force generation is uncorrelated with the amount of kinetochore-colocalized Stu2. These and other data imply that Stu2 colocalizes with kinetochores by recognizing growing microtubule plus ends within yeast kinetochores. We propose that Stu2 destabilizes these plus ends to indirectly contribute to the "catch-bond" activity of the kinetochores.
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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.