2KDD

Solution structure of the conserved C-terminal dimerization domain of Borealin

Summary for 2KDD

• Entry DOI: 10.2210/pdb2kdd/pdb
• NMR Information: BMRB: 16110
• Descriptor: Borealin (1 entity in total)
• Functional Keywords: protein dimer, cell cycle, cell division, centromere, chromosomal protein, cytoplasm, mitosis, nucleus, phosphoprotein, polymorphism
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 16164.31

Authors

Lingel, A.,Bourhis, E.,Cochran, A.G.,Fairbrother, W.J. (deposition date: 2009-01-06, release date: 2009-06-30, Last modification date: 2024-05-08)

Primary citation

Bourhis, E.,Lingel, A.,Phung, Q.,Fairbrother, W.J.,Cochran, A.G.
Phosphorylation of a borealin dimerization domain is required for proper chromosome segregation.
Biochemistry, 48:6783-6793, 2009

PubMed Abstract: 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.

PubMed: 19530738
DOI: 10.1021/bi900530v

Experimental method

SOLUTION NMR