Related Experiment Video
Updated: May 1, 2026

Real-Time Monitoring of Aurora kinase A Activation using Conformational FRET Biosensors in Live Cells
Published on: July 30, 2020
A novel mechanism for activation of Aurora-A kinase by Ajuba
Meirong Bai1, Jun Ni1, Jiaxue Wu1
1State Key Laboratory of Genetic Engineering, Institute of Genetics, School of Life Sciences, Fudan University, 220 Handan Road, Shanghai, People's Republic of China.
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.
More Related Videos
07:49Characterize Disease-related Mutants of RAF Family Kinases by Using a Set of Practical and Feasible Methods
Published on: July 17, 2019
11:20An Integrated System to Remotely Trigger Intracellular Signal Transduction by Upconversion Nanoparticle-mediated Kinase Photoactivation
Published on: August 30, 2017
Related Concept Videos
Anaphase Promoting Complex
Anaphase Promoting Complex
The JAK-STAT Signaling Pathway
cAMP-dependent Protein Kinase Pathways
PI3K/mTOR/AKT Signaling Pathway
MAPK Signaling Cascades