title: Regulation of aurora B kinase by the lipid raft protein flotillin-1.
abstract: 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.
authors.affiliation: Unitat de Recerca Biomèdica, Institut de Recerca Hospital Vall d'Hebrón, 08035 Barcelona, Spain.
authors.forename: Valentí
authors.initials: V
authors.lastname: Gómez
authors.forename: Marta
authors.initials: M
authors.lastname: Sesé
authors.forename: Anna
authors.initials: A
authors.lastname: Santamaría
authors.forename: Juan D
authors.initials: JD
authors.lastname: Martínez
authors.forename: Elisabet
authors.initials: E
authors.lastname: Castellanos
authors.forename: Marta
authors.initials: M
authors.lastname: Soler
authors.forename: Timothy M
authors.initials: TM
authors.lastname: Thomson
authors.forename: Rosanna
authors.initials: R
authors.lastname: Paciucci
mesh_terms: D000111:Acetylcysteine / Q000031:analogs & derivatives / Q000494:pharmacology; D000900:Anti-Bacterial Agents / Q000494:pharmacology; D064107:Aurora Kinase B; D064127:Aurora Kinases; D017675:CREST Syndrome / Q000097:blood; D002455:Cell Division; D002467:Cell Nucleus / Q000502:physiology; D017931:DNA Primers; D015536:Down-Regulation; D055785:Gene Knockdown Techniques; D006367:HeLa Cells; D006801:Humans; D020287:In Situ Nick-End Labeling; D051034:Inhibitor of Apoptosis Proteins; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism / Q000494:pharmacology*; D008869:Microtubule-Associated Proteins / Q000494:pharmacology; D009842:Oligopeptides / Q000494:pharmacology; D017346:Protein Serine-Threonine Kinases / Q000172:deficiency / Q000187:drug effects / Q000235:genetics* / Q000378:metabolism*; D034741:RNA, Small Interfering / Q000737:chemistry / Q000235:genetics; D020133:Reverse Transcriptase Polymerase Chain Reaction; D000077022:Survivin; D014162:Transfection
chemical_list: D000900:Anti-Bacterial Agents; C107489:BIRC5 protein, human; D017931:DNA Primers; D051034:Inhibitor of Apoptosis Proteins; D008565:Membrane Proteins; D008869:Microtubule-Associated Proteins; D009842:Oligopeptides; D034741:RNA, Small Interfering; D000077022:Survivin; C106354:flotillins; C067713:lactacystin; C576921:AURKB protein, human; D064107:Aurora Kinase B; D064127:Aurora Kinases; D017346:Protein Serine-Threonine Kinases; D000111:Acetylcysteine; C078846:epoxomicin