The Borealin Dimerization Domain Interacts with Sgo1 to Drive Aurora B-mediated Spindle Assembly.

The Borealin Dimerization Domain Interacts with Sgo1 to Drive Aurora B-mediated Spindle Assembly. Mol Biol Cell. 2020 Jul 22;:mbcE20050341 Authors: Bonner MK, Haase J, Saunders H, Gupta H, Li BI, Kelly AE Abstract 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 directly interacts with the dimerization domain of the CPC subunit Borealin. Borealin and the PP2A phosphatase complex can simultaneously bind 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 (SAC) 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 that promote the proper interaction between spindle microtubules and chromosomes. PMID: 32697622 [PubMe...
Source: Mol Biol Cell - Category: Molecular Biology Authors: Tags: Mol Biol Cell Source Type: research