ArticleMolecular biology of the cell2016
Molecular basis of Kar9-Bim1 complex function during mating and spindle positioning.
Article in Molecular biology of the cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 25 citations in OpenAlex.
- A small signaling domain controls PPIP5K phosphatase activity in phosphate homeostasis.Nature communications · 2025Article
- Phase separation of a microtubule plus-end tracking protein into a fluid fractal network.Nature communications · 2025Article
- The roles of yeast formins and their regulators Bud6 and Bil2 in the pheromone response.Molecular biology of the cell · 2024Article
- Nuclear Fusion in Yeast and Plant Reproduction.Plants (Basel, Switzerland) · 2023Article
- Systematic analysis of microtubule plus-end networks defines EB-cargo complexes critical for mitosis in budding yeast.Molecular biology of the cell · 2023Article
- Multivalency ensures persistence of a +TIP body at specialized microtubule ends.Nature cell biology · 2023Article
- Cargo Recognition Mechanisms of Yeast Myo2 Revealed by AlphaFold2-Powered Protein Complex Prediction.Biomolecules · 2022Article
- Microtubule plus-ends act as physical signaling hubs to activate RhoA during cytokinesis.eLife · 2019Article
- Nuclear movement in fungi.Seminars in cell & developmental biology · 2018Review
- NOD is a plus end-directed motor that binds EB1 via a new microtubule tip localization sequence.The Journal of cell biology · 2018Article
- An unconventional interaction between Dis1/TOG and Mal3/EB1 in fission yeast promotes the fidelity of chromosome segregation.Journal of cell science · 2016Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Kar9 pathway promotes nuclear fusion during mating and spindle alignment during metaphase in budding yeast. How Kar9 supports the different outcome of these two divergent processes is an open question. Here, we show that three sites in the C-terminal disordered domain of Kar9 mediate tight Kar9 interaction with the C-terminal dimerization domain of Bim1 (EB1 orthologue). Site1 and Site2 contain SxIP motifs; however, Site3 defines a novel type of EB1-binding site. Whereas Site2 and Site3 mediate Kar9 recruitment to microtubule tips, nuclear movement and karyogamy, solely Site2 functions in spindle positioning during metaphase. Site1 in turn plays an inhibitory role during mating. Additionally, the Kar9-Bim1 complex is involved in microtubule-independent activities during mating. Together, our data reveal how multiple and partially redundant EB1-binding sites provide a microtubule-associated protein with the means to modulate its biochemical properties to promote different molecular processes during cell proliferation and differentiation.
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Registered trials
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