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Updated: Jul 14, 2026
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Real-Time Monitoring of Aurora kinase A Activation using Conformational FRET Biosensors in Live Cells
Published on: July 30, 2020
Mitotic kinase Aurora-A phosphorylates RASSF1A and modulates RASSF1A-mediated microtubule interaction and M-phase
R Rong1, L Y Jiang, M S Sheikh
1Department of Pharmacology, State University of New York, Upstate Medical University, Syracuse, NY 13210, USA.
Oncogene
|June 15, 2007
Summary
This study identifies Aurora-A as the first kinase to phosphorylate the RASSF1A tumor suppressor. Aurora-A phosphorylation disrupts RASSF1A
Area of Science:
- Cell Biology
- Molecular Oncology
- Cancer Research
Background:
- RAS-association domain family 1, isoform A (RASSF1A) is a tumor suppressor involved in microtubule stabilization and M-phase cell cycle arrest.
- Mitotic phosphorylation regulates microtubule-associated proteins, but RASSF1A phosphorylation during mitosis remains largely uncharacterized.
Purpose of the Study:
- To identify the kinase responsible for RASSF1A phosphorylation during mitosis.
- To investigate the functional consequences of RASSF1A phosphorylation on its interaction with microtubules and cell cycle regulation.
Main Methods:
- Identification of Aurora-A as a RASSF1A kinase through interaction and phosphorylation assays.
- Site-directed mutagenesis to mimic constitutive phosphorylation at Threonine202/Serine203.
- Assessment of RASSF1A-microtubule interactions and cell cycle arrest.
- Evaluation of Aurora-A overexpression effects on RASSF1A-mediated growth suppression.
Main Results:
- Aurora-A directly interacts with and phosphorylates RASSF1A at Threonine202 and/or Serine203.
- Phosphorylation-mimicking mutations disrupt RASSF1A-microtubule binding and abolish M-phase cell cycle arrest.
- Aurora-A overexpression interferes with RASSF1A's tumor-suppressive functions.
Conclusions:
- Aurora-A is a novel kinase for RASSF1A, linking an oncogenic mitotic kinase to this tumor suppressor.
- Aurora-A-mediated phosphorylation regulates RASSF1A's microtubule interactions and M-phase cell cycle control.
- This phosphorylation mechanism offers a new target for cancer therapy.
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