title: pavarotti encodes a kinesin-like protein required to organize the central spindle and contractile ring for cytokinesis.
abstract: Mutations in the Drosophila gene pavarotti result in the formation of abnormally large cells in the embryonic nervous system. In mitotic cycle 16, cells of pav mutant embryos undergo normal anaphase but then develop an abnormal telophase spindle and fail to undertake cytokinesis. We show that the septin Peanut, actin, and the actin-associated protein Anillin, do not become correctly localized in pav mutants. pav encodes a kinesin-like protein, PAV-KLP, related to the mammalian MKLP-1. In cellularized embryos, the protein is localized to centrosomes early in mitosis, and to the midbody region of the spindle in late anaphase and telophase. We show that Polo kinase associates with PAV-KLP with which it shows an overlapping pattern of subcellular localization during the mitotic cycle and this distribution is disrupted in pav mutants. We suggest that PAV-KLP is required both to establish the structure of the telophase spindle to provide a framework for the assembly of the contractile ring, and to mobilize mitotic regulator proteins.
authors.affiliation: Cancer Research Campaign (CRC) Laboratories, Cell Cycle Genetics Research Group, Department of Anatomy and Physiology, Medical Sciences Institute, University of Dundee, Dundee DD1 4HN, UK. d.m.glover@dundee.ac.uk
authors.forename: R R
authors.initials: RR
authors.lastname: Adams
authors.forename: A A
authors.initials: AA
authors.lastname: Tavares
authors.forename: A
authors.initials: A
authors.lastname: Salzberg
authors.forename: H J
authors.initials: HJ
authors.lastname: Bellen
authors.forename: D M
authors.initials: DM
authors.lastname: Glover
mesh_terms: D000199:Actins / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D002455:Cell Division / Q000235:genetics*; D048429:Cell Size; D018385:Centrosome / Q000648:ultrastructure; D003001:Cloning, Molecular; D003285:Contractile Proteins / Q000378:metabolism; D029721:Drosophila Proteins; D004331:Drosophila melanogaster / Q000166:cytology / Q000196:embryology / Q000235:genetics*; D004625:Embryo, Nonmammalian / Q000648:ultrastructure; D017344:Genes, Insect; D019476:Insect Proteins / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D008322:Mammals / Q000378:metabolism; D008840:Microfilament Proteins; D008869:Microtubule-Associated Proteins / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D008969:Molecular Sequence Data; D009420:Nervous System / Q000166:cytology / Q000196:embryology*; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D013045:Species Specificity; D008941:Spindle Apparatus / Q000648:ultrastructure*; D013347:Subcellular Fractions / Q000737:chemistry; D013692:Telophase / Q000235:genetics*
chemical_list: D000199:Actins; D003285:Contractile Proteins; D029721:Drosophila Proteins; D019476:Insect Proteins; D008840:Microfilament Proteins; D008869:Microtubule-Associated Proteins; C095886:anillin; C490516:pav protein, Drosophila; C087195:pnut protein, Drosophila; C072004:polo protein, Drosophila; D017346:Protein Serine-Threonine Kinases