title: Drosophila Aurora A kinase is required to localize D-TACC to centrosomes and to regulate astral microtubules.
abstract: 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.
authors.affiliation: Department of Genetics, Cancer Research Campaign Cell Cycle Genetics Group, University of Cambridge, Cambridge CB2 3EH, UK.
authors.forename: Régis
authors.initials: R
authors.lastname: Giet
authors.forename: Doris
authors.initials: D
authors.lastname: McLean
authors.forename: Simon
authors.initials: S
authors.lastname: Descamps
authors.forename: Michael J
authors.initials: MJ
authors.lastname: Lee
authors.forename: Jordan W
authors.initials: JW
authors.lastname: Raff
authors.forename: Claude
authors.initials: C
authors.lastname: Prigent
authors.forename: David M
authors.initials: DM
authors.lastname: Glover
mesh_terms: D000255:Adenosine Triphosphate / Q000235:genetics / Q000378:metabolism; D000818:Animals; D064127:Aurora Kinases; D001665:Binding Sites / Q000235:genetics; D002451:Cell Compartmentation / Q000502:physiology; D018797:Cell Cycle Proteins; D018385:Centrosome / Q000201:enzymology*; D004330:Drosophila / Q000196:embryology / Q000235:genetics / Q000378:metabolism*; D029721:Drosophila Proteins / Q000235:genetics / Q000378:metabolism; D005260:Female; D008297:Male; D008869:Microtubule-Associated Proteins / Q000235:genetics / Q000378:metabolism*; D008870:Microtubules / Q000201:enzymology* / Q000235:genetics; D008938:Mitosis / Q000235:genetics*; D009154:Mutation / Q000235:genetics; D009687:Nuclear Proteins / Q000235:genetics / Q000378:metabolism; D011494:Protein Kinases / Q000235:genetics / Q000378:metabolism*; D017346:Protein Serine-Threonine Kinases; D017434:Protein Structure, Tertiary / Q000235:genetics; D012313:RNA / Q000235:genetics / Q000378:metabolism; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism; D008941:Spindle Apparatus / Q000201:enzymology* / Q000235:genetics; D029867:Xenopus Proteins
chemical_list: C486738:CKAP5 protein, Xenopus; D018797:Cell Cycle Proteins; D029721:Drosophila Proteins; D008869:Microtubule-Associated Proteins; D009687:Nuclear Proteins; D011993:Recombinant Fusion Proteins; C404402:TACC protein, Drosophila; D029867:Xenopus Proteins; C121511:msps protein, Drosophila; D012313:RNA; D000255:Adenosine Triphosphate; D011494:Protein Kinases; C112134:AURKA protein, Xenopus; D064127:Aurora Kinases; D017346:Protein Serine-Threonine Kinases