ArticleThe Journal of biological chemistry2012
Post-translational modifications regulate assembly of early spindle orientation complex in yeast.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Asymmetric distribution of glucose transporter mRNA provides a growth advantage in yeast.The EMBO journal · 2019Article
- Nuclear movement in fungi.Seminars in cell & developmental biology · 2018Review
- Molecular basis of Kar9-Bim1 complex function during mating and spindle positioning.Molecular biology of the cell · 2016Article
- Emerging roles of sumoylation in the regulation of actin, microtubules, intermediate filaments, and septins.Cytoskeleton (Hoboken, N.J.) · 2015Review
- Aurora B spatially regulates EB3 phosphorylation to coordinate daughter cell adhesion with cytokinesis.The Journal of cell biology · 2013Article
- Purification, crystallization and preliminary crystallographic analysis of Kar9p from Saccharomyces cerevisiae.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mitosis begins with the tethering of chromosomes to the mitotic spindle and their orientation perpendicular to the axis of cell division. In budding yeast, mitotic spindle orientation and the subsequent chromosome segregation are two independent processes. Early spindle orientation is driven by the actin-bound myosin Myo2p, which interacts with the adapter Kar9p. The latter also binds to microtubule-associated Bim1p, thereby connecting both types of cytoskeleton. This study focuses on the interaction between Kar9p and Bim1p and its regulation. We solved the crystal structure of the previously reported Kar9p-binding motif of Bim1p and identified a second, novel Kar9p interaction domain. We further show that two independent post-translational modification events regulate their interaction. Whereas Kar9p sumoylation is required for efficient complex formation with Bim1p, Aurora B/Ipl1p-dependent phosphorylation of Bim1p down-regulates their interaction. The observed effects of these modifications allow us to propose a novel regulatory framework for the assembly and disassembly of the early spindle orientation complex.
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Registered trials
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