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Disruption of the function of the A-type Aurora kinase of Drosophila by mutation or RNAi leads to a reduction in the length of astral microtubules in syncytial embryos, larval neuroblasts, and cultured S2 cells. In neuroblasts, it can also lead to loss of an organized centrosome and its associated aster from one of the spindle poles, whereas the centrosome at the other pole has multiple centrioles. When centrosomes are present at the poles of aurA mutants or aurA RNAi spindles, they retain many antigens but are missing the Drosophila counterpart of mammalian transforming acidic coiled coil (TACC) proteins, D-TACC. We show that a subpopulation of the total Aurora A is present in a complex with D-TACC, which is a substrate for the kinase. We propose that one of the functions of Aurora A kinase is to direct centrosomal organization such that D-TACC complexed to the MSPS/XMAP215 microtubule-associated protein may be recruited, and thus modulate the behavior of astral microtubules.

Original publication

DOI

10.1083/jcb.200108135

Type

Journal article

Journal

J Cell Biol

Publication Date

04/02/2002

Volume

156

Pages

437 - 451

Keywords

Adenosine Triphosphate, Animals, Aurora Kinases, Binding Sites, Cell Compartmentation, Cell Cycle Proteins, Centrosome, Drosophila, Drosophila Proteins, Female, Male, Microtubule-Associated Proteins, Microtubules, Mitosis, Mutation, Nuclear Proteins, Protein Kinases, Protein Structure, Tertiary, Protein-Serine-Threonine Kinases, RNA, Recombinant Fusion Proteins, Spindle Apparatus, Xenopus Proteins