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MBC in Press, published online ahead of print June 3, 2009
Mol. Biol. Cell 10.1091/mbc.E09-05-0370

A more recent version of this article appeared on August 1, 2009
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Submitted on May 6, 2009
Revised on May 19, 2009
Accepted on May 22, 2009

Molecular Distinctions between Aurora A and B: A Single Residue Change Transforms Aurora A into Correctly Localized and Functional Aurora B

Fabienne Hans,*{dagger} Dimitrios A. Skoufias,{dagger}{ddagger} Stefan Dimitrov,* and Robert L. Margolis{ddagger}{sect}

*INSERM, Université Joseph Fourier - Grenoble 1, and Institut Albert Bonniot U823, Site Santé-BP 170, 38042 Grenoble, France; {ddagger}Institut de Biologie Structurale Jean Pierre Ebel (CEA/CNRS/UJF), 38027 Grenoble Cedex 1, France; {sect}Sidney Kimmel Cancer Center, San Diego, CA 92121

Monitoring Editor: Daniel J. Lew

Aurora A and Aurora B, paralogue mitotic kinases, share highly similar primary sequence. Both are important to mitotic progression, but their localizations and functions are distinct. We have combined shRNA suppression with overexpression of Aurora mutants to address the cause of the distinction between Aurora A and Aurora B. Aurora A residue G198, mutated to Asparagine to mimic the aligned N142 of Aurora B, causes Aurora A to bind the Aurora B binding partner INCENP, but not the Aurora A binding partner TPX2. The mutant Aurora A rescues Aurora B mitotic function. We conclude that binding to INCENP is alone critical to the distinct function of Aurora B. Although G198 of Aurora A is required for TPX2 binding, N142G Aurora B retains INCENP binding and Aurora B function. Thus, while a single residue change transforms Aurora A, the reciprocal mutation of Aurora B does not create Aurora A function. An Aurora A-{Delta}120 N-terminal truncation construct reinforces Aurora A similarity to Aurora B, as it does not associate with centrosomes, but instead associates with kinetochores.

{dagger}These authors have contributed equally to this work.

Address correspondence to: Robert L. Margolis (stefan.dimitrov{at}ujf-grenoble.fr)






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