Aurora-C and Aurora-B share phosphorylation and regulation of CENP-A and Borealin during mitosis

Scott D. Slattery; Rebecca V. Moore; Bill R. Brinkley; Rebecca Hall

doi:10.4161/cc.7.6.5563

Aurora-C and Aurora-B share phosphorylation and regulation of CENP-A and Borealin during mitosis

Scott D. Slattery, Rebecca V. Moore, Bill R. Brinkley, Rebecca Hall

Research output: Contribution to journal › Article › peer-review

42 Scopus citations

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)
Pages (from-to)	787-795
Number of pages	9
Journal	Cell Cycle
Volume	7
Issue number	6
DOIs	https://doi.org/10.4161/cc.7.6.5563
State	Published - Mar 15 2008

Keywords

Aurora-C
Borealin
CENP-A
Chromosomal passenger complex
Mitosis

ASJC Scopus subject areas

Cell Biology
Biochemistry
Molecular Biology

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title = "Aurora-C and Aurora-B share phosphorylation and regulation of CENP-A and Borealin during mitosis",

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.",

keywords = "Aurora-C, Borealin, CENP-A, Chromosomal passenger complex, Mitosis",

author = "Slattery, {Scott D.} and Moore, {Rebecca V.} and Brinkley, {Bill R.} and Rebecca Hall",

note = "Funding Information: We thank Takeshi Urano, Aaron VanHooser, Rebecca Heald, Subrata Sen, Michael Mancini and Jerome Rattner for generously providing reagents. We also thank Denae Nash for helpful discussions and Thuy-Ai Nguyen for technical assistance. This work was supported by NIH Grant CA 41424 to B.R.B. and The Huffington Foundation Research Fund to B.R.B. and R.A.M.",

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AU - Slattery, Scott D.

AU - Moore, Rebecca V.

AU - Brinkley, Bill R.

AU - Hall, Rebecca

N1 - Funding Information: We thank Takeshi Urano, Aaron VanHooser, Rebecca Heald, Subrata Sen, Michael Mancini and Jerome Rattner for generously providing reagents. We also thank Denae Nash for helpful discussions and Thuy-Ai Nguyen for technical assistance. This work was supported by NIH Grant CA 41424 to B.R.B. and The Huffington Foundation Research Fund to B.R.B. and R.A.M.

PY - 2008/3/15

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N2 - 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.

AB - 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.

KW - Aurora-C

KW - Borealin

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KW - Chromosomal passenger complex

KW - Mitosis

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Aurora-C and Aurora-B share phosphorylation and regulation of CENP-A and Borealin during mitosis

Abstract

Keywords

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