The Borealin dimerization domain interacts with Sgo1 to drive Aurora B–mediated spindle assembly
Autor: | Alexander E. Kelly, Mary Kate Bonner, Hayden Saunders, Julian Haase, Hindol Gupta, Biyun Iris Li |
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Rok vydání: | 2020 |
Předmět: |
Chromosomal passenger complex
Chromosomal Proteins Non-Histone Aurora B kinase Mitosis Cell Cycle Proteins macromolecular substances Spindle Apparatus Computational biology Xenopus Proteins Biology Microtubules Domain (software engineering) Xenopus laevis Chromosome Segregation Animals Aurora Kinase B Phosphorylation Kinetochores Molecular Biology technology industry and agriculture Cell Biology embryonic structures Molecular mechanism M Phase Cell Cycle Checkpoints Brief Reports Dimerization Signal Transduction |
Zdroj: | Molecular Biology of the Cell |
ISSN: | 1939-4586 1059-1524 |
DOI: | 10.1091/mbc.e20-05-0341 |
Popis: | The chromosomal passenger complex (CPC), which includes the kinase Aurora B, is a master regulator of meiotic and mitotic processes that ensure the equal segregation of chromosomes. Sgo1 is thought to play a major role in the recruitment of the CPC to chromosomes, but the molecular mechanism and contribution of Sgo1-dependent CPC recruitment is currently unclear. Using Xenopus egg extracts and biochemical reconstitution, we found that Sgo1 interacts directly with the dimerization domain of the CPC subunit Borealin. Borealin and the PP2A phosphatase complex can bind simultaneously to the coiled-coil domain of Sgo1, suggesting that Sgo1 can integrate Aurora B and PP2A activities to modulate Aurora B substrate phosphorylation. A Borealin mutant that specifically disrupts the Sgo1–Borealin interaction results in defects in CPC chromosomal recruitment and Aurora B–dependent spindle assembly, but not in spindle assembly checkpoint signaling at unattached kinetochores. These findings establish a direct molecular connection between Sgo1 and the CPC and have major implications for the different functions of Aurora B, which promote the proper interaction between spindle microtubules and chromosomes. |
Databáze: | OpenAIRE |
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