The tricornered gene, which is required for the integrity of epidermal cell extensions, encodes the Drosophila nuclear DBF2-related kinase.
During their differentiation epidermal cells of Drosophila form a rich variety of polarized structures. These include the epidermal hairs that decorate much of the adult cuticular surface, the shafts of the bristle sense organs, the lateral extensions of the arista, and the larval denticles. These cuticular structures are produced by cytoskeletal-mediated outgrowths of epidermal cells. Mutations in the tricornered gene result in the splitting or branching of all of these structures. Thus, tricornered function appears to be important for maintaining the integrity of the outgrowths. tricornered mutations however do not have major effects on the growth or shape of these cellular extensions. Inhibiting actin polymerization in differentiating cells by cytochalasin D or latrunculin A treatment also induces the splitting of hairs and bristles, suggesting that the actin cytoskeleton might be a target of tricornered. However, the drugs also result in short, fat, and occasionally malformed hairs and bristles. The data suggest that the function of the actin cytoskeleton is important for maintaining the integrity of cellular extensions as well as their growth and shape. Thus, if tricornered causes the splitting of cellular extensions by interacting with the actin cytoskeleton it likely does so in a subtle way. Consistent with this possibility we found that a weak tricornered mutant is hypersensitive to cytochalasin D. We have cloned the tricornered gene and found that it encodes the Drosophila NDR kinase. This is a conserved ser/thr protein kinase found in Caenorhabditis elegans and humans that is related to a number of kinases that have been found to be important in controlling cell structure and proliferation.
Geng
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Biology Department and Cancer Center, University of Virginia, Charlottesville, Virginia 22903, USA.
He
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Wang
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Adler
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D000199:Actins / Q000378:metabolism; D000483:Alleles; D000595:Amino Acid Sequence; D000825:Animal Structures / Q000648:ultrastructure; D000818:Animals; D002467:Cell Nucleus / Q000201:enzymology*; D016764:Cell Polarity; D003001:Cloning, Molecular; D003599:Cytoskeleton / Q000648:ultrastructure; D029721:Drosophila Proteins; D004331:Drosophila melanogaster / Q000201:enzymology / Q000235:genetics* / Q000254:growth & development; D000078404:Epidermal Cells; D004817:Epidermis / Q000201:enzymology; D004847:Epithelial Cells / Q000201:enzymology / Q000648:ultrastructure; D017344:Genes, Insect; D006801:Humans; D019476:Insect Proteins / Q000235:genetics* / Q000502:physiology; D007814:Larva; D009024:Morphogenesis / Q000187:drug effects; D005810:Multigene Family; D016254:Mutagenesis, Insertional; D010641:Phenotype; D017346:Protein Serine-Threonine Kinases / Q000235:genetics* / Q000502:physiology; D011679:Pupa; D015842:Serine Proteinase Inhibitors / Q000494:pharmacology; D013045:Species Specificity; D014404:Tubulin / Q000378:metabolism; D014747:Vinblastine / Q000494:pharmacology; D014921:Wings, Animal / Q000648:ultrastructure
D000199:Actins; D029721:Drosophila Proteins; D019476:Insect Proteins; D015842:Serine Proteinase Inhibitors; D014404:Tubulin; D014747:Vinblastine; C419769:trc protein, Drosophila; D017346:Protein Serine-Threonine Kinases