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Human Molecular Genetics Advance Access published online on October 23, 2006
Human Molecular Genetics, doi:10.1093/hmg/ddl410
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© The Author 2006. Published by Oxford University Press. All rights reserved
Received August 30, 2006
Revised September 25, 2006
Accepted October 6, 2006

Article

The N-terminal domain of the Aurora-A Phe-31 variant encodes an E3 ubiquitin ligase and mediates ubiquitination of I{kappa}B{alpha}

Paraskevi Briassouli 1, Florence Chan 2, and Spiros Linardopoulos 3 *

1 The Breakthrough Breast Cancer Research Centre, The Institute of Cancer Research Fulham Road, London SW3 6JB, UK; UCSF Comprehensive Cancer Center, Box 0875, 2340 Sutter St., San Francisco, CA 94143, USA
2 Cancer Research UK Centre for Cancer Therapeutics, The Institute of Cancer Research, Haddow's Laboratories, 15 Cotswold Road, Sutton SM2 5NG, UK
3 The Breakthrough Breast Cancer Research Centre, The Institute of Cancer Research Fulham Road, London SW3 6JB, UK; Cancer Research UK Centre for Cancer Therapeutics, The Institute of Cancer Research, Haddow's Laboratories, 15 Cotswold Road, Sutton SM2 5NG, UK

* To whom correspondence should be addressed.
Spiros Linardopoulos, E-mail: spiros.linardopoulos{at}icr.ac.uk


  Abstract

Aurora-A is important regulator of mitosis and is frequently amplified in human cancer. Ectopic expression of Aurora-A in mammalian cells induces centrosome amplification, genomic instability and transformation. A common genetic variant in Aurora-A (F31I) is preferentially amplified and is associated with the occurrence and the status of colon, oesophageal and breast cancers. Here we demonstrate that the N-terminal domain of Aurora-A Phe-31 variant exhibits an intrinsic ubiquitin ligase activity. Mutation of cysteines 8, 33 and 49 of Aurora-A abolishes the ubiquitin ligase activity of the protein. Aurora-A in a complex with UBE2N/MMS2 catalyses polyubiquitination of I{kappa}B{alpha} in vitro and in vivo.


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