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Human Molecular Genetics Advance Access originally published online on October 23, 2006
Human Molecular Genetics 2006 15(22):3343-3350; doi:10.1093/hmg/ddl410
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© The Author 2006. Published by Oxford University Press. All rights reserved. For Permissions, please email: journals.permissions@oxfordjournals.org

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 Briassouli1,{dagger}, Florence Chan2 and Spiros Linardopoulos1,2,*

1 The Breakthrough Breast Cancer Research Centre, The Institute of Cancer Research, Fulham Road, London SW3 6JB, UK and 2 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. Tel: +44 2071435341; Fax: +44 2071435340; Email: spiros.linardopoulos{at}icr.ac.uk

Received August 30, 2006; Revised September 25, 2006; Accepted October 6, 2006

Aurora-A is an 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.

{dagger} Present address: UCSF Comprehensive Cancer Center, PO Box 0875, 2340 Sutter St, San Francisco, CA 94143, USA.


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