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Author (up) Cram, E.J.; Shang, H.; Schwarzbauer, J.E. file  url
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  Title A systematic RNA interference screen reveals a cell migration gene network in C. elegans Type Journal Article
  Year 2006 Publication Journal of Cell Science Abbreviated Journal J Cell Sci  
  Volume 119 Issue Pt 23 Pages 4811-4818  
  Keywords Animals; Animals, Genetically Modified; Caenorhabditis elegans/embryology/*genetics; Cell Movement/*genetics; *Gene Regulatory Networks; Genes, Helminth; Gonads/embryology; Phenotype; *RNA Interference  
  Abstract Cell migration is essential during embryonic development and tissue morphogenesis. During gonadogenesis in the nematode Caenorhabditis elegans, migration of the distal tip cells forms two U-shaped gonad arms. Malformation results if the distal tip cells stop prematurely or follow an aberrant path, and abnormalities are easily visualized in living nematodes. Here we describe the first comprehensive in vivo RNA interference screen for genes required for cell migration. In this non-biased screen, we systematically analyzed 16,758 RNA-interference depletion experiments by light microscopy and identified 99 genes required for distal tip cell migration. Genetic and physical interaction data connect 59 of these genes to form a cell migration gene network that defines distal tip cell migration in vivo.  
  Call Number Serial 1705  
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Author (up) Sakube, Y.; Ando, H.; Kagawa, H. file  url
doi  openurl
  Title An abnormal ketamine response in mutants defective in the ryanodine receptor gene ryr-1 (unc-68) of Caenorhabditis elegans Type Journal Article
  Year 1997 Publication Journal of Molecular Biology Abbreviated Journal J Mol Biol  
  Volume 267 Issue 4 Pages 849-864  
  Keywords Amino Acid Sequence; Anesthetics, Dissociative/*pharmacology; Animals; Animals, Genetically Modified; Aspartic Acid/pharmacology; Caenorhabditis elegans/*drug effects/genetics/physiology; Calcium Channels/analysis/*genetics/metabolism; Cloning, Molecular; Gene Expression; Genes, Helminth/*genetics; Ketamine/*pharmacology; Molecular Sequence Data; Muscle Contraction/drug effects; Muscle Proteins/analysis/*genetics/metabolism; Mutation; N-Methylaspartate/pharmacology; Organ Specificity; Phosphorylation; Receptors, N-Methyl-D-Aspartate/agonists/antagonists & inhibitors; Recombinant Fusion Proteins/analysis; Ryanodine Receptor Calcium Release Channel; Sequence Analysis, DNA; Sequence Homology, Amino Acid  
  Abstract To characterize excitation-contraction coupling in Caenorhabditis elegans, we applied two approaches. First, we isolated a mutant having abnormal responses to ketamine, an anesthetic in vertebrates. The novel mutation unc-68(kh30) (isolated as kra-1(kh30)), exhibited strict ketamine-dependent convulsions followed by paralysis. Second, we cloned the C. elegans ryanodine receptor gene ryr-1 that is located near the center of chromosome V. ryr-1 consists of 46 exons, which encode a predicted protein of 5071 amino acid residues that is homologous to Drosophila and vertebrate ryanodine receptors. ryr-1 promoter/lacZ plasmids were expressed in body-wall and pharyngeal muscles. Non-muscle cell expression may be seen with a truncated promoter. In addition, we show that the unc-68/kra-1(kh30) mutation is a Ser1444 Asn substitution at a putative protein kinase C phosphorylation site in ryr-1, and that unc-68(e540) contains a splice acceptor mutation that creates a premature stop codon in the ryr-1 gene. We confirmed that unc-68(e540) is a mutation in ryr-1 by injecting the complete ryr-1 gene into unc-68(e540) animals and recovering wild-type progeny. Results presented here will be useful in studying the structure and function of ryanodine receptors in excitation-contraction coupling and in understanding the evolution of ryanodine receptor tissue specificity.  
  Call Number Serial 448  
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Author (up) Thacker, C.; Rose, A.M. file  url
doi  openurl
  Title A look at the Caenorhabditis elegans Kex2/Subtilisin-like proprotein convertase family Type Journal Article
  Year 2000 Publication BioEssays : News and Reviews in Molecular, Cellular and Developmental Biology Abbreviated Journal Bioessays  
  Volume 22 Issue 6 Pages 545-553  
  Keywords Animals; Caenorhabditis elegans/*enzymology/genetics; Genes, Helminth; Humans; Multigene Family; Mutation; Phylogeny; *Proprotein Convertases; *Saccharomyces cerevisiae Proteins; Subtilisins/chemistry/genetics/*metabolism  
  Abstract Significant advances have recently been made in our understanding of the mechanisms of activation of proteins that require processing. Often this involves endoproteolytic cleavage of precursor forms at basic residues, and is carried out by a group of serine endoproteinases, termed the proprotein convertases. In mammals, seven different convertases have been identified to date. These act in both the regulated secretory pathway for the processing of prohormones and proneuropeptides and in the constitutive secretory pathway, in which a variety of proproteins are activated endoproteolytically. The recently completed sequence of the nematode Caenorhabditis elegans genome affords a unique opportunity to examine the entire proprotein convertase family in a multicellular organism. Here we review the nature of the family, emphasising the structural features, characteristic of the four nematode genes, that supply all of the necessary functions unique to this group of serine endoproteinases. Studies of the C. elegans genes not only provide important information about the evaluation of this gene family but should help to illuminate the roles of these proteins in mammalian systems. BioEssays 22:545-553, 2000.  
  Call Number Serial 522  
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