Publication Abstract from PubMed
The chromosomal passenger complex (CPC) has been identified as a master regulator of mitosis. In particular, proper chromosome segregation and cytokinesis depend on the correct localization and function of the CPC. Within the complex, the kinase Aurora B associates with Incenp, Survivin and Borealin. The stoichiometry of the complex as well as a complete understanding of how these four components interact with each other remains to be elucidated. Here, we identify a new domain of Borealin. We determined its structure using NMR spectroscopy and discovered a novel dimerization motif. Interestingly, we found that substitutions at Borealin T230, recently identified as an Mps1 phosphorylation site, can modulate the dimerization state of Borealin. Mutation of this single residue to alanine or valine impairs Aurora B activity during mitosis and causes chromosome segregation defects. This study reveals that Mps1 regulates the CPC through a novel Borealin domain.
Phosphorylation of a Borealin dimerization domain is required for proper chromosome segregation.,Bourhis E, Lingel A, Phung Q, Fairbrother WJ, Cochran AG Biochemistry. 2009 Jun 17. PMID:19530738[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
