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  • IP3 signalling regulates exogenous RNAi in Caenorhabditis elegans
    1. Anikó I Nagy14,
    2. Rafael P Vázquez‐Manrique2,3,,
    3. Marie Lopez15,
    4. Christo P Christov1,
    5. María Dolores Sequedo2,3,
    6. Mareike Herzog16,
    7. Anna E Herlihy17,
    8. Maxime Bodak18,
    9. Roxani Gatsi19 and
    10. Howard A Baylis*,1
    1. 1Department of Zoology, University of Cambridge, Cambridge, UK
    2. 2Research Group in Molecular, Cellular and Genomic Biomedicine, Health Research Institute‐La Fe, Valencia, Spain
    3. 3Centre for Biomedical Network Research on Rare Diseases (CIBERER), Valencia, Spain
    4. 4Heart and Vascular Centre, Semmelweis University, Budapest, Hungary
    5. 5 Unit Human Evolutionary Genetics, Institut Pasteur, Paris, France
    6. 6 Wellcome Trust Sanger Institute, Cambridge, UK
    7. 7 MRC Laboratory for Molecular Cell Biology, University College London, London, UK
    8. 8 ETH Zurich, Institute of Molecular Health Sciences, Zurich, Switzerland
    9. 9 Centro Andaluz de Biología del Desarrollo (CABD), Universidad Pablo de Olavide, Sevilla, Spain
    1. *Corresponding author. Tel: +44 1223 336630; Fax: +44 1223 336676; E‐mail: hab28{at}cam.ac.uk
    1. These authors contributed equally to this work

    Reducing intracellular IP3 signaling enhances RNAi sensitivity in C. elegans through a function of IP3 in the intestine. This suggests that an animal's physiology or environment may influence its RNAi responses.

    Synopsis

    Reducing intracellular IP3 signaling enhances RNAi sensitivity in C. elegans through a function of IP3 in the intestine. This suggests that an animal's physiology or environment may influence its RNAi responses.

    • Altering intracellular IP3 signalling modifies sensitivity to RNAi in different tissues.

    • Tissue‐specific rescue experiments suggest IP3 functions in the intestine to control RNAi sensitivity throughout the animal.

    • IP3 signalling mutations can further enhance the sensitivity of existing RNAi hypersensitive strains.

    • C. elegans
    • calcium signalling
    • enhanced RNAi
    • inositol 1,4,5‐trisphosphate
    • RNA interference
    • Received September 15, 2014.
    • Revision received December 4, 2014.
    • Accepted December 15, 2014.
    Anikó I Nagy, Rafael P Vázquez‐Manrique, Marie Lopez, Christo P Christov, María Dolores Sequedo, Mareike Herzog, Anna E Herlihy, Maxime Bodak, Roxani Gatsi, Howard A Baylis
  • Plasticity of PI4KIIIα interactions at the plasma membrane
    1. Jeeyun Chung1,
    2. Fubito Nakatsu1,
    3. Jeremy M Baskin1 and
    4. Pietro De Camilli*,1
    1. 1Department of Cell Biology, Howard Hughes Medical Institute Program in Cellular Neuroscience, Neurodegeneration and Repair Yale University Medical School, New Haven, CT, USA
    1. *Corresponding author. Tel: +1 203 737 4461; E‐mail: pietro.decamilli{at}yale.edu

    TMEM150A, a homologue of yeast Sfk1, interacts with the PIPI4KIIIα–EFR3 complex at the plasma membrane and positively regulates PI(4,5)P2 synthesis. It affects the composition of the PI4KIIIα complex, revealing a plasticity of the molecular interactions that control PI4KIIIα localization and function.

    Synopsis

    TMEM150A, a homologue of yeast Sfk1, interacts with the PIPI4KIIIα–EFR3 complex at the plasma membrane and positively regulates PI(4,5)P2 synthesis. It affects the composition of the PI4KIIIα complex, revealing a plasticity of the molecular interactions that control PI4KIIIα localization and function.

    • TMEM150A is the mammalian homologue of yeast Sfk1 and like Sfk1 interacts with a PI 4‐kinase, PI4KIIIα.

    • It forms a complex with PI4KIIIα and EFR3, which is mutually exclusive with the presence of TTC7 in the complex.

    • Overexpression of TMEM150A enhances the rate of PI(4,5)P2 recovery following PI(4,5)P2 depletion.

    • phospholipase C
    • PI4KA
    • Rolling blackout
    • Ypp1
    • Received June 11, 2014.
    • Revision received December 17, 2014.
    • Accepted December 17, 2014.

    This is an open access article under the terms of the Creative Commons Attribution‐NonCommercial‐NoDerivs 4.0 License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non‐commercial and no modifications or adaptations are made.

    Jeeyun Chung, Fubito Nakatsu, Jeremy M Baskin, Pietro De Camilli
  • Response to Stephen Holgate
    1. Lutz Bornmann (bornmann{at}gv.mpg.de) 1 and
    2. Loet Leydesdorff (loet{at}leydesdorff.net) 2
    1. 1Division for Science and Innovation Studies, Administrative Headquarters of the Max Planck Society, Munich, Germany
    2. 2Amsterdam School of Communication Research (ASCoR) University of Amsterdam, Amsterdam, The Netherlands

    Response to Stephen Holgate.

    Lutz Bornmann, Loet Leydesdorff
  • A comment on “Scientometrics in a changing research landscape”
    1. Stephen T Holgate (s.holgate{at}soton.ac.uk) 1,2
    1. 1Faculty of Medicine, Southampton General Hospital, Southampton, UK
    2. 2 Chair on behalf of Main Panel A of REF 2014

    A comment on “Scientometrics in a changing research landscape”.

    Stephen T Holgate
  • Glycolytic enzymes localize to ribonucleoprotein granules in Drosophila germ cells, bind Tudor and protect from transposable elements
    1. Ming Gao1,,
    2. Travis C Thomson2,,
    3. T Michael Creed1,
    4. Shikui Tu3,
    5. Sudan N Loganathan1,
    6. Christina A Jackson1,
    7. Patrick McCluskey1,
    8. Yanyan Lin1,
    9. Scott E Collier4,
    10. Zhiping Weng3,
    11. Paul Lasko5,
    12. Melanie D Ohi4 and
    13. Alexey L Arkov*,1
    1. 1Department of Biological Sciences, Murray State University, Murray, KY, USA
    2. 2Program in Molecular Medicine, University of Massachusetts Medical School, Worcester, MA, USA
    3. 3Program in Bioinformatics and Integrative Biology, University of Massachusetts Medical School, Worcester, MA, USA
    4. 4Department of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, TN, USA
    5. 5Department of Biology, McGill University, Montreal, QC, Canada
    1. *Corresponding author. Tel: +1 270 809 6053; E‐mail: aarkov{at}murraystate.edu
    1. Co‐first authors

    Glycolytic enzymes localize to ribonucleoprotein granules in Drosophila germ cells, the genomes of which they protect from the expression of transposable elements. The enzymes also associate with the germ granule Tudor protein.

    Synopsis

    Glycolytic enzymes localize to ribonucleoprotein granules in Drosophila germ cells, the genomes of which they protect from the expression of transposable elements. The enzymes also associate with the germ granule Tudor protein.

    • Glycolytic enzymes localize to ribonucleoprotein granules in germ cells and protect the germline from transposable elements.

    • In granules, ATP‐producing glycolytic enzymes are located in the vicinity of ATP‐dependent RNA helicases.

    • The first EM structure of the full‐length Tudor protein and its binding to glycolytic enzymes are reported.

    • germ cells
    • glycolysis
    • stem cells
    • transposable elements
    • Tudor domain
    • Received October 6, 2014.
    • Revision received December 2, 2014.
    • Accepted December 9, 2014.
    Ming Gao, Travis C Thomson, T Michael Creed, Shikui Tu, Sudan N Loganathan, Christina A Jackson, Patrick McCluskey, Yanyan Lin, Scott E Collier, Zhiping Weng, Paul Lasko, Melanie D Ohi, Alexey L Arkov
  • Epigenetic predisposition to reprogramming fates in somatic cells
    1. Maayan Pour1,,
    2. Inbar Pilzer1,,
    3. Roni Rosner1,
    4. Zachary D Smith2,
    5. Alexander Meissner2 and
    6. Iftach Nachman*,1
    1. 1Department of Biochemistry and Molecular Biology, Tel Aviv University, Tel Aviv, Israel
    2. 2Department of Stem Cell and Regenerative Biology, Harvard University, Cambridge, MA, USA
    1. *Corresponding author. Tel: +972 3 640 5900; E‐mail: iftachn{at}post.tau.ac.il
    1. Equal contribution

    The potential of Mouse Embryonic Fibroblasts (MEFs) to generate iPSCs is determined before OKSM induction and symmetrically maintained over the short term. Epigenetic perturbations of MEFs can alter their future response to reprogramming.

    Synopsis

    The potential of mouse embryonic fibroblasts (MEFs) to generate iPSCs is determined before OKSM induction and symmetrically maintained over the short term. Epigenetic perturbations of MEFs can alter their future response to reprogramming.

    • The potential to generate iPSC colonies is shared between sister lineages emanating from a pre‐induction cell division.

    • Cell‐specific OKSM levels or local niche effects do not explain preference toward iPSC fate.

    • Perturbing H3K27 or H3K4 methylation marks prior to OKSM induction increases the number of iPSC lineages.

    • cell fate decisions
    • live‐cell imaging
    • reprogramming
    • Received July 3, 2014.
    • Revision received December 11, 2014.
    • Accepted December 12, 2014.
    Maayan Pour, Inbar Pilzer, Roni Rosner, Zachary D Smith, Alexander Meissner, Iftach Nachman
  • Lessons learned in GermanyIn the past decade, Germany has invested a great deal of money into science funding schemes that have markedly changed its research landscape. Was the money well spent, and how will it be spent in future?

    In the past decade, Germany has invested a great deal of money into science funding schemes that have markedly changed its research landscape. Was the money well spent, and how will it be spent in future?

    1. Katrin Weigmann, Freelance Journalist (mail{at}k-weigmann.de) 1
    1. 1 Oldenburg, Germany

    More than a decade ago, Germany began to reform its universities and public research endeavours with concomitant increased investment in research. The country has made some progress, but challenges remain to further improve the quality of scientific research at German universities.

    Katrin Weigmann