Regulation of Aurora B Kinase by the Lipid Raft Protein Flotillin-1

The lipid raft protein Flotillin-1 was previously shown to be required for cell proliferation. Here we show that it is critical for the maintenance of the levels of the mitotic regulator Aurora B. Knockdown of Flotillin-1 induced aberrant mitotic events similar to those produced by Aurora B depletio...

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Bibliographic Details
Published in:The Journal of biological chemistry 2010-07, Vol.285 (27), p.20683-20690
Main Authors: Gómez, Valentí, Sesé, Marta, Santamaría, Anna, Martínez, Juan D., Castellanos, Elisabet, Soler, Marta, Thomson, Timothy M., Paciucci, Rosanna
Format: Article
Language:English
Subjects:
Acetylcysteine - analogs & derivatives
Acetylcysteine - pharmacology
Anti-Bacterial Agents - pharmacology
Aurora B
Aurora Kinase B
Aurora Kinases
Cell Biology
Cell Cycle
Cell Division
Cell Nucleus - physiology
CREST Syndrome - blood
DNA Primers
Down-Regulation
Flotillin
Gene Knockdown Techniques
Gene Regulation
HeLa Cells
Humans
In Situ Nick-End Labeling
Inhibitor of Apoptosis Proteins
Lipid Raft
Membrane Proteins - genetics
Membrane Proteins - metabolism
Membrane Proteins - pharmacology
Microtubule-Associated Proteins - pharmacology
Mitosis
Oligopeptides - pharmacology
Protein-Protein Interactions
Protein-Serine-Threonine Kinases - deficiency
Protein-Serine-Threonine Kinases - drug effects
Protein-Serine-Threonine Kinases - genetics
Protein-Serine-Threonine Kinases - metabolism
Reverse Transcriptase Polymerase Chain Reaction
RNA Silencing
RNA, Small Interfering - chemistry
RNA, Small Interfering - genetics
Survivin
Transfection
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Summary:The lipid raft protein Flotillin-1 was previously shown to be required for cell proliferation. Here we show that it is critical for the maintenance of the levels of the mitotic regulator Aurora B. Knockdown of Flotillin-1 induced aberrant mitotic events similar to those produced by Aurora B depletion and led to a marked decline in Aurora B levels and activity. Transfection of wild-type full-length Flotillin-1 or forms directed to the nucleus increased Aurora B levels and activity. Flotillin-1 interacted with Aurora B directly through its SPFH domain in a complex distinct from the chromosomal passenger protein complex, and the two proteins co-purified in nuclear, non-raft fractions. These observations are the first evidence for a function of Flotillin-1 outside of lipid rafts and suggest its critical role in the maintenance of a pool of active Aurora B.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M110.130591