Hsp90 is required to localise cyclin B and Msps/ch-TOG to the mitotic spindle in Drosophila and humans.

Journal article

During mitosis, cyclin B is extremely dynamic and although it is concentrated at the centrosomes and spindle microtubules (MTs) in organisms ranging from yeast to humans, the mechanisms that determine its localisation are poorly understood. To understand how cyclin B is targeted to different locations in the cell we have isolated proteins that interact with cyclin B in Drosophila embryo extracts. Here we show that cyclin B interacts with the molecular chaperone Hsp90 and with the MT-associate...

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Authors: Basto, R; Gergely, F; Draviam, V; Ohkura, H; Liley, K

• Publication status: Published
• Journal: Journal of cell science
• Volume: 120
• Issue: Pt 7
• Pages: 1278-1287
• Publication date: 2007-04-01
• DOI: 10.1242/jcs.000604
• EISSN: 1477-9137
• ISSN: 0021-9533
• Language: English
• Keywords: HSP90 Heat-Shock Proteins; Recombinant Fusion Proteins; Protein Binding; Drosophila; Humans; Microtubule-Associated Proteins; Drosophila Proteins; Cyclin B; Embryo, Nonmammalian; Animals; Mitotic Spindle Apparatus