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Updated: Jun 10, 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
SUMOylation modulates the function of Aurora-B kinase.
Gonzalo Fernández-Miranda1, Ignacio Pérez de Castro, Mar Carmena
1Cell Division and Cancer Group, Spanish National Cancer Research Center (CNIO), Madrid, Spain.
Journal of Cell Science
|July 29, 2010
Summary
SUMOylation of Aurora B kinase is crucial for proper cell division. This modification regulates Aurora B
Area of Science:
- Cell Biology
- Molecular Biology
- Genetics
Background:
- Aurora kinases regulate key mitotic events, including spindle assembly and chromosome segregation.
- Aurora B, a component of the chromosomal passenger complex (CPC), is vital for kinetochore-microtubule attachments and cytokinesis.
Purpose of the Study:
- To investigate the role of SUMOylation in Aurora B kinase function.
- To determine how SUMO modification affects Aurora B localization and activity during mitosis.
Main Methods:
- In vitro binding assays to assess SUMO peptide interaction with Aurora B.
- Site-directed mutagenesis to create a SUMO-deficient Aurora B mutant (Aurora B(K207R)).
- Analysis of mitotic defects, chromosome segregation, and CPC localization in cells expressing wild-type versus mutant Aurora B.
Main Results:
- Aurora B possesses a SUMO modification motif and binds SUMO peptides in vitro when complexed with INCENP.
- Mutation of Lys207 to arginine (Aurora B(K207R)) prevents in vivo SUMOylation.
- SUMO-null Aurora B expression leads to abnormal chromosome segregation, cytokinesis failure, and altered CPC localization, without reducing kinase activity.
Conclusions:
- SUMOylation of Aurora B is essential for its proper function, likely by regulating its localization.
- Altered SUMOylation affects CPC distribution, leading to mitotic errors.
- SUMOylation may mediate the removal of CPC from chromosome arms during prometaphase.
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