The Borealin dimerization domain interacts with Sgo1 to drive Aurora B-mediated spindle assembly.

Molecular Biology of the Cell
Mary Kate BonnerAlexander E Kelly

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 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.

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Citations

Dec 7, 2020·Cytoskeleton·Joseph Y OngJorge Z Torres
Mar 30, 2021·Frontiers in Molecular Biosciences·Shan-Shan JiangXing-Wei Xie
Apr 10, 2021·The Journal of Cell Biology·Lin-Ing WangKim S McKim
May 26, 2021·Cancer Science·Minji JoToru Hirota

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Methods Mentioned

BETA
two-hybrid
Y2H
equilibrium binding assay
pulldown
immunoprecipitation
pull down
immunoprecipitations
Two
in vitro transcription
NMR

Software Mentioned

ImageStudio
NIS Elements
NIS Elements AR
Fiji ImageJ
Jalview
GraphPad Prism
Prism GraphPad
Clustalx
Fiji

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