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Eukaryotic Cell, May 2008, p. 894-905, Vol. 7, No. 5
1535-9778/08/$08.00+0     doi:10.1128/EC.00422-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Dictyostelium Aurora Kinase Has Properties of both Aurora A and Aurora B Kinases{triangledown} ,{dagger}

Hui Li,1 Qian Chen,1,{ddagger} Markus Kaller,2 Wolfgang Nellen,2 Ralph Gräf,3 and Arturo De Lozanne1*

Section of Molecular Cell & Developmental Biology and Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, Texas 78712,1 Abt. Genetik, Universität Kassel, Heinrich-Plett-Str. 40, 34132 Kassel, Germany,2 Universität Potsdam, Institut für Biochemie und Biologie, Zellbiologie, Karl-Liebknecht-Str. 24-25, Haus 26, 14476 Potsdam-Golm, Germany3

Received 19 November 2007/ Accepted 27 February 2008

Aurora kinases are highly conserved proteins with important roles in mitosis. Metazoans contain two kinases, Aurora A and B, which contribute distinct functions at the spindle poles and the equatorial region respectively. It is not currently known whether the specialized functions of the two kinases arose after their duplication in animal cells or were already present in their ancestral kinase. We show that Dictyostelium discoideum contains a single Aurora kinase, DdAurora, that displays characteristics of both Aurora A and B. Like Aurora A, DdAurora has an extended N-terminal domain with an A-box sequence and localizes at the spindle poles during early mitosis. Like Aurora B, DdAurora binds to its partner DdINCENP and localizes on centromeres at metaphase, the central spindle during anaphase, and the cleavage furrow at the end of cytokinesis. DdAurora also has several unusual properties. DdAurora remains associated with centromeres in anaphase, and this association does not require an interaction with DdINCENP. DdAurora then localizes at the cleavage furrow, but only at the end of cytokinesis. This localization is dependent on DdINCENP and the motor proteins Kif12 and myosin II. Thus, DdAurora may represent the ancestral kinase that gave rise to the different Aurora kinases in animals and also those in other organisms.

* Corresponding author. Mailing address: Molecular Cell and Developmental Biology, University of Texas at Austin, 1 University Station C-1000, Austin TX 78712. Phone: (512) 232-6100. Fax: (512) 471-3878. E-mail: a.delozanne{at}mail.utexas.edu

{triangledown} Published ahead of print on 7 March 2008.

{dagger} Supplemental material for this article may be found at http://ec.asm.org/.

{ddagger} Present address: Department of Molecular, Cellular and Developmental Biology, Yale University, New Haven, CT 06511.

Eukaryotic Cell, May 2008, p. 894-905, Vol. 7, No. 5
1535-9778/08/$08.00+0     doi:10.1128/EC.00422-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Fu, J., Bian, M., Liu, J., Jiang, Q., Zhang, C. (2009). A single amino acid change converts Aurora-A into Aurora-B-like kinase in terms of partner specificity and cellular function. Proc. Natl. Acad. Sci. USA 106: 6939-6944 [Abstract] [Full Text]  


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