Spatio-temporal control of Aurora-A in the cell cycle through its binding partners

Spatio-temporal control of Aurora-A in the cell cycle through its binding partners

Professor Richard Bayliss; University of Leeds

Richard Bayliss studied Natural Sciences at the University of Cambridge, and then completed his PhD in molecular biology at the MRC Laboratory of Molecular Biology in Cambridge in the group of Murray Stewart. After a 1-year stint as a Research Fellow at Trinity College, Cambridge, he was an EMBO Long Term Fellow with Elena Conti at the European Molecular Biology Laboratory in Heidelberg, Germany, and then a Research Fellow in the group of Gabriel Waksman in Birkbeck College, London. He established his independent research group at the Institute of Cancer Research in London in 2006, funded by a Royal Society Research Fellowship and Cancer Research UK. He relocated to the University of Leicester in 2011 and then to the University of Leeds in 2016 to take up his current position as Professor of Molecular Medicine and a member of the Astbury Centre for Structural Molecular Biology.

Aurora-A is an essential cell cycle kinase with critical roles in mitotic entry and spindle dynamics. These functions require binding partners such as CEP192 and TPX2, which modulate both Aurora-A kinase activity and localisation. We have determined the structure and role of these distinct Aurora-A complexes and discovered how they act within the context of the wider molecular network. We propose an evolutionarily conserved spatial hierarchy, which protects against genome instability through fine-tuning and correctly localising Aurora-A activity. Aurora-A contributes to genome stability via another mechanism in cancer cells, through its interaction with members of the MYC family of transcription factors. We are exploring the potential for cancer-specific targeting of protein-protein interactions of Aurora-A as an alternative to ATP-competitive inhibitors.

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