| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 2816359 | Gene | 2014 | 7 Pages |
•PreLIM of Ajuba interacts with Cd of Aurora A, not with the full length.•PreLIM domain can activate Cd of Aurora A, but not the full length.•LIM can competitively bind with Aurora-A Nt, preventing its binding with Cd.•PreLIM domain is phosphorylated by C-terminal kinase domain of Aurora-A.•Suggest a novel model for Aurora-A regulation by Ajuba
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.
