Identification of the auto-inhibitory domains of Aurora-A kinase

Biochem Biophys Res Commun. 2007 Jun 1;357(2):347-52. doi: 10.1016/j.bbrc.2007.03.129. Epub 2007 Mar 30.


Aurora-A is a centrosome-localized serine/threonine kinase that is overexpressed in multiple human cancers. Here, we report an intramolecular inhibitory regulation in Aurora-A between its N-terminal regulatory domain (aa 1-128, Nt) and the C-terminal catalytic domain (aa 129-403, Cd). Removal of Nt results in a significant increase in kinase activity. Nt inhibited the activity of the single C-terminal kinase domain, but had little effect on the activity of the full-length of Aurora-A. PP1 is not involved in this regulation, instead, Nt interacts Cd directly in vitro and in vivo. The non-Aurora box (aa 64-128) in the N-terminal negatively regulated the kinase activity of the C-terminal kinase domain by intramolecular interaction with aa 240-300 within the C-terminal.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aurora Kinases
  • Binding Sites
  • Cell Line
  • Enzyme Activation
  • Enzyme Inhibitors / chemistry
  • Enzyme Inhibitors / metabolism
  • Humans
  • Kidney / chemistry*
  • Kidney / metabolism*
  • Protein Binding
  • Protein Serine-Threonine Kinases / chemistry*
  • Protein Serine-Threonine Kinases / metabolism*
  • Protein Structure, Tertiary
  • Structure-Activity Relationship


  • Enzyme Inhibitors
  • Aurora Kinases
  • Protein Serine-Threonine Kinases