Abstract
Aurora-B and -C kinases are members of the Aurora serine/threonine kinase family of mitotic regulators. Aurora-B kinase is evolutionarily conserved from yeast to humans and has multiple functions in chromosome condensation, cohesion, biorientation and in cytokinesis. In contrast, Aurora-C kinase has only been found in mammals, is upregulated in some tumor cell lines and tissues, and has a unique physiological role in spermiogenesis. Despite these known functions, little is known about the function of Aurora-C in mitosis. We have found that Aurora-C interacts with Borealin in addition to the other known members of the Aurora-B chromosomal passenger complex (CPC). We have also found that Aurora-C, like Aurora-B, phosphorylates the centromeric histone Centromere Protein-A (CENP-A) and Borealin in vitro. These molecular mechanisms are consistent with our observation that in the absence of Aurora-B, Aurora-C is sufficient for proper mitotic phosphorylation of CENP-A and centromeric localization of the CPC proteins. Thus, Aurora-C shares Aurora-B substrates and is capable of performing mitotic functions previously attributed only to Aurora-B.
Original language | English (US) |
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Pages (from-to) | 787-795 |
Number of pages | 9 |
Journal | Cell Cycle |
Volume | 7 |
Issue number | 6 |
DOIs | |
State | Published - Mar 15 2008 |
Keywords
- Aurora-C
- Borealin
- CENP-A
- Chromosomal passenger complex
- Mitosis
ASJC Scopus subject areas
- Cell Biology
- Biochemistry
- Molecular Biology