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Updated: Jul 15, 2026

Real-Time Monitoring of Aurora kinase A Activation using Conformational FRET Biosensors in Live Cells
Published on: July 30, 2020
Phosphorylation by aurora-B negatively regulates survivin function during mitosis.
Sally P Wheatley1, Rachel M Barrett, Paul D Andrews
1Genome Damage and Stability Centre, University of Sussex, Falmer, Brighton, UK. s.p.wheatley@sussex.ac.uk
Phosphorylation of survivin at threonine 117 by aurora B kinase is vital for mitosis. Dephosphorylation of survivin after mitosis is crucial for cell division and progression into anaphase.
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- Survivin, a key mitotic regulator, forms a complex with aurora B kinase.
- Aurora B kinase phosphorylates survivin at threonine 117 (T117) in vitro.
- The in vivo functional significance of survivin phosphorylation at T117 during mitosis remains unclear.
Purpose of the Study:
- To investigate the role of survivin phosphorylation at T117 by aurora B kinase in regulating survivin function during mitosis in vivo.
- To determine the impact of T117 phosphorylation status on survivin's localization and function in cell division.
Main Methods:
- Utilized a phospho-specific antibody to detect T117-phosphorylated survivin during mitosis.
- Employed two independent RNA interference (RNAi) complementation strategies using survivin mutants (T117A and T117E).
- Performed fluorescence imaging and fluorescence recovery after photobleaching (FRAP) to assess protein localization and dynamics.
Main Results:
- Confirmed T117 phosphorylation of survivin during mitosis and its presence at the midbody during cytokinesis.
- Demonstrated that non-phosphorylatable survivin (T117A) could rescue wild-type function, but phosphomimic survivin (T117E) failed to restore viability or complement defects.
- Showed that survivin(T117E) exhibited reduced affinity for centromeres compared to survivin(T117A).
Conclusions:
- Survivin phosphorylation at T117 occurs during mitosis and is regulated by aurora B kinase.
- Dephosphorylation of survivin post-phosphorylation is essential for proper chromosome congression and anaphase progression.
- T117 phosphorylation status critically influences survivin's centromeric localization and mitotic function.
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