A novel mechanism for activation of Aurora-A kinase by Ajuba |
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| Authors: | Meirong Bai Jun Ni Jiaxue Wu Bin Wang Suqin Shen Long Yu |
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| Affiliation: | 1. State Key Laboratory of Genetic Engineering, Institute of Genetics, School of Life Sciences, Fudan University, 220 Handan Road, Shanghai, People''s Republic of China;2. School of Computer Science, Fudan University, 220 Handan Road, Shanghai, People''s Republic of China |
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| 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. |
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| Keywords: | aa, amino acid(s) cDNA, DNA complementary to RNA kDa, kilodalton(s) wt, wild type PMSF, phenylmethylsulfonyl fluoride PAGE, PA-gel electrophoresis Nt, N-terminal regulatory domain (aa 1&ndash 128) of Aurora-A Cd, C-terminal catalytic domain (aa 129&ndash 403) of Aurora-A P-T288, autophosphorylation of Thr288 GST, glutathione S-transferase PBS, phosphate-buffered saline EGFP, enhanced green fluorescent protein |
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