![]() |
|
|
A more recent version of this article appeared on January 1, 2005
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Submitted on June 4, 2004
Revised on September 22, 2004
Accepted on October 13, 2004

||
*Institut Albert Bonniot, Institut National de la Santé et de la Recherche Médicale, 38706 La Tronche cedex, France;
Institut de Biologie Structurale Jean Pierre Ebel (Commissariat à l’Energie Atomique/Centre National de la Recherche Scientifique), 38027 Grenoble cedex 1, France;
Institut de Génétique et de Biologie Moléculaire et Cellulaire, Centre National de la Recherche Scientifique - Institut National de la Santé et de la Recherche Médicale -Université Louis Pasteur, 67404 Illkirch-Strasbourg, France
Monitoring Editor: J. Richard McIntosh
Aurora B, a protein kinase required in mitosis, localizes to inner centromeres at metaphase and the spindle midzone in anaphase and is required for proper chromosome segregation and cytokinesis. Aurora A, a paralogue of Aurora B, localizes instead to centrosomes and spindle microtubules. Except for distinct N-termini, Aurora B and Aurora A have highly similar sequences. We have combined siRNA ablation of Aurora B with overexpression of truncation mutants to investigate the role of Aurora B sequence in its function. Reintroduction of Aurora B during siRNA treatment restored its localization and function. This permitted a restoration of function test to determine the sequence requirements for Aurora B targeting and function. Using this rescue protocol, neither N-terminal truncation of Aurora B unique sequence nor substitution with Aurora A N-terminal sequence affected Aurora B localization or function. Truncation of unique Aurora B C-terminal sequence from terminal residue 344 to residue 333 was without effect, but truncation to 326 abolished localization and function. Deletion of residues 326-333 completely abolished localization and blocked cells at prometaphase, establishing this sequence as critical to Aurora B function. Our findings thus establish a small sequence as essential for the distinct localization and function of Aurora B.
These authors contributed equally to this work.
||Corresponding authors.
E-mail: stefan.dimitrov{at}ujf-grenoble.fr E-mail: Margolis{at}ibs.fr
This article has been cited by other articles:
![]() |
F. Hans, D. A. Skoufias, S. Dimitrov, and R. L. Margolis Molecular Distinctions between Aurora A and B: A Single Residue Change Transforms Aurora A into Correctly Localized and Functional Aurora B Mol. Biol. Cell, August 1, 2009; 20(15): 3491 - 3502. [Abstract] [Full Text] [PDF] |
||||
![]() |
J. Fu, M. Bian, J. Liu, Q. Jiang, and C. Zhang A single amino acid change converts Aurora-A into Aurora-B-like kinase in terms of partner specificity and cellular function PNAS, April 28, 2009; 106(17): 6939 - 6944. [Abstract] [Full Text] [PDF] |
||||
![]() |
Z. Yue, A. Carvalho, Z. Xu, X. Yuan, S. Cardinale, S. Ribeiro, F. Lai, H. Ogawa, E. Gudmundsdottir, R. Gassmann, et al. Deconstructing Survivin: comprehensive genetic analysis of Survivin function by conditional knockout in a vertebrate cell line J. Cell Biol., October 20, 2008; 183(2): 279 - 296. [Abstract] [Full Text] [PDF] |
||||
![]() |
K. Monier, S. Mouradian, and K. F. Sullivan DNA methylation promotes Aurora-B-driven phosphorylation of histone H3 in chromosomal subdomains J. Cell Sci., January 1, 2007; 120(1): 101 - 114. [Abstract] [Full Text] [PDF] |
||||
![]() |
H. G. Nguyen, D. Chinnappan, T. Urano, and K. Ravid Mechanism of Aurora-B Degradation and Its Dependency on Intact KEN and A-Boxes: Identification of an Aneuploidy-Promoting Property Mol. Cell. Biol., June 15, 2005; 25(12): 4977 - 4992. [Abstract] [Full Text] [PDF] |
||||