A novel mechanism for activation of Aurora-A kinase by Ajuba

Gene. 2014 Jun 10;543(1):133-9. doi: 10.1016/j.gene.2014.03.048. Epub 2014 Mar 26.

Abstract

Aurora-A is a centrosome-localized serine/threonine kinase, which plays a critical role in mitotic and meiotic cell division processes. However, the regulation of Aurora-A is still not fully understood. Previously, we have found an intramolecular inhibitory regulation mechanism of Aurora-A: the N-terminal regulatory domain (aa 1-128, Nt) can interact with the C-terminal catalytic domain (aa 129-403, Cd) and inhibit the kinase activity of Aurora-A. In this study, we found that the PreLIM domain of Ajuba, another important activator of Aurora-A, induces the autophosphorylation of the C-terminal kinase domain of Aurora-A, and is phosphorylated by the C-terminal. Moreover, the LIM domain of Ajuba can competitively bind to the N-terminal of Aurora-A, and inhibited the interaction between N-terminal and C-terminal of Aurora A. Taken together, these results suggest a novel mechanism for regulation of Aurora-A by Ajuba.

Keywords: Ajuba; Aurora-A; Autophosphorylation; Mitosis; Protein interaction.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aurora Kinase A / chemistry
  • Aurora Kinase A / genetics
  • Aurora Kinase A / metabolism*
  • Binding, Competitive
  • Enzyme Activation
  • HEK293 Cells
  • HeLa Cells
  • Humans
  • LIM Domain Proteins / chemistry
  • LIM Domain Proteins / metabolism*
  • Phosphorylation
  • Protein Binding
  • Protein Interaction Domains and Motifs
  • Protein Interaction Mapping

Substances

  • AJUBA protein, human
  • LIM Domain Proteins
  • Aurora Kinase A