title: The Caenorhabditis elegans Aurora B kinase AIR-2 phosphorylates and is required for the localization of a BimC kinesin to meiotic and mitotic spindles.
abstract: BimC kinesins are required for mitotic spindle assembly in a variety of organisms. These proteins are localized to centrosomes, spindle microtubules, and the spindle midzone. We have previously shown that the Caenorhabditis elegans Aurora B kinase AIR-2 is required for the localization of the ZEN-4 kinesin protein to midzone microtubules. To determine whether the association of BimC kinesins with spindle microtubules is also dependent on AIR-2, we examined the expression pattern of BMK-1, a C. elegans BimC kinesin, in wild-type and AIR-2-deficient embryos. BMK-1 is highly expressed in the hermaphrodite gonad and is localized to meiotic spindle microtubules in the newly fertilized embryo. In mitotic embryos, BMK-1 is associated with spindle microtubules from prophase through anaphase and is concentrated at the spindle midzone during anaphase and telophase. In the absence of AIR-2, BMK-1 localization to meiotic and mitotic spindles is greatly reduced. This is not a consequence of loss of ZEN-4 localization because BMK-1 is appropriately localized in ZEN-4-deficient embryos. Furthermore, AIR-2 and BMK-1 directly interact with one another and the C-terminal tail domain of BMK-1 is specifically phosphorylated by AIR-2 in vitro. Together with our previous data, these results suggest that at least one function of the Aurora B kinases is to recruit spindle-associated motor proteins to their sites of action.
authors.affiliation: Department of Molecular Genetics, The University of Texas M. D. Anderson Cancer Center, Houston, TX 77030, USA.
authors.forename: John D
authors.initials: JD
authors.lastname: Bishop
authors.forename: Zhenbo
authors.initials: Z
authors.lastname: Han
authors.forename: Jill M
authors.initials: JM
authors.lastname: Schumacher
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D064107:Aurora Kinase B; D064127:Aurora Kinases; D015153:Blotting, Western; D017173:Caenorhabditis elegans / Q000201:enzymology / Q000235:genetics / Q000378:metabolism*; D029742:Caenorhabditis elegans Proteins / Q000378:metabolism / Q000502:physiology*; D017124:Conserved Sequence; D004625:Embryo, Nonmammalian; D005982:Glutathione Transferase / Q000378:metabolism; D015801:Helminth Proteins / Q000378:metabolism*; D007150:Immunohistochemistry; D016547:Kinesins / Q000378:metabolism / Q000502:physiology*; D048054:Mitogen-Activated Protein Kinase 7 / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D008938:Mitosis; D008969:Molecular Sequence Data; D010766:Phosphorylation; D017354:Point Mutation; D011233:Precipitin Tests; D017346:Protein Serine-Threonine Kinases / Q000172:deficiency / Q000378:metabolism / Q000502:physiology*; D017434:Protein Structure, Tertiary; D034622:RNA Interference; D011994:Recombinant Proteins / Q000096:biosynthesis; D017386:Sequence Homology, Amino Acid; D008941:Spindle Apparatus; D013696:Temperature; D013912:Threonine / Q000737:chemistry; D020798:Two-Hybrid System Techniques
chemical_list: D029742:Caenorhabditis elegans Proteins; D015801:Helminth Proteins; D011994:Recombinant Proteins; C114455:ZEN-4 protein, C elegans; D013912:Threonine; D005982:Glutathione Transferase; D064107:Aurora Kinase B; D064127:Aurora Kinases; D017346:Protein Serine-Threonine Kinases; C491506:air-2 protein, C elegans; D048054:Mitogen-Activated Protein Kinase 7; C000605617:BMK-1 protein, C elegans; D016547:Kinesins