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  • 1
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    Kinases and phosphatases--a marriage is consummated (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-06-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hafen, E -- New York, N.Y. -- Science. 1998 May 22;280(5367):1212-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Zoologisches Institut der Universitat Zurich, Zurich, Switzerland. hafen@zool.unizh.ch〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9634402" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/metabolism ; Calcium-Calmodulin-Dependent Protein Kinase Type 4 ; Calcium-Calmodulin-Dependent Protein Kinases/metabolism ; Cyclic AMP Response Element-Binding Protein/metabolism ; Down-Regulation ; Dual Specificity Phosphatase 6 ; Enzyme Activation ; Mitogen-Activated Protein Kinase 1 ; Phosphoprotein Phosphatases/*metabolism ; Phosphorylation ; Protein Kinases/*metabolism ; Protein Tyrosine Phosphatases/metabolism ; *Signal Transduction
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    Extension of life-span by loss of CHICO, a Drosophila insulin receptor substrate protein (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-04-09
    Description: The Drosophila melanogaster gene chico encodes an insulin receptor substrate that functions in an insulin/insulin-like growth factor (IGF) signaling pathway. In the nematode Caenorhabditis elegans, insulin/IGF signaling regulates adult longevity. We found that mutation of chico extends fruit fly median life-span by up to 48% in homozygotes and 36% in heterozygotes. Extension of life-span was not a result of impaired oogenesis in chico females, nor was it consistently correlated with increased stress resistance. The dwarf phenotype of chico homozygotes was also unnecessary for extension of life-span. The role of insulin/IGF signaling in regulating animal aging is therefore evolutionarily conserved.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Clancy, D J -- Gems, D -- Harshman, L G -- Oldham, S -- Stocker, H -- Hafen, E -- Leevers, S J -- Partridge, L -- New York, N.Y. -- Science. 2001 Apr 6;292(5514):104-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University College London, Wolfson House, 4 Stephenson Way, London NW1 2HE, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11292874" target="_blank"〉PubMed〈/a〉
    Keywords: Aging/*physiology ; Alleles ; Animals ; Body Constitution ; Carrier Proteins/genetics/metabolism ; Crosses, Genetic ; *Drosophila Proteins ; Drosophila melanogaster/genetics/*physiology ; Female ; Fertility ; Genes, Insect ; Heterozygote ; Hot Temperature ; Insect Proteins/*genetics/*metabolism ; Insulin/metabolism ; Insulin Receptor Substrate Proteins ; *Intracellular Signaling Peptides and Proteins ; Longevity/*physiology ; Male ; Mutation ; Oxidative Stress ; Protein-Tyrosine Kinases/genetics/metabolism ; *Receptor Protein-Tyrosine Kinases ; Receptor, Insulin/*metabolism ; Reproduction ; Signal Transduction ; Somatomedins/metabolism ; Starvation ; Superoxide Dismutase
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    Drosophila S6 kinase: a regulator of cell size (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-09-25
    Description: Cell proliferation requires cell growth; that is, cells only divide after they reach a critical size. However, the mechanisms by which cells grow and maintain their appropriate size have remained elusive. Drosophila deficient in the S6 kinase gene (dS6K) exhibited an extreme delay in development and a severe reduction in body size. These flies had smaller cells rather than fewer cells. The effect was cell-autonomous, displayed throughout larval development, and distinct from that of ribosomal protein mutants (Minutes). Thus, the dS6K gene product regulates cell size in a cell-autonomous manner without impinging on cell number.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Montagne, J -- Stewart, M J -- Stocker, H -- Hafen, E -- Kozma, S C -- Thomas, G -- F32 GM15926/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1999 Sep 24;285(5436):2126-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Friedrich Miescher Institute, Maulbeerstrasse 66, 4058 Basel, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10497130" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Body Constitution ; Cell Count ; Cell Division ; Cell Size ; Drosophila melanogaster/cytology/*enzymology/genetics/*growth & development ; Epithelial Cells/cytology ; Female ; Genes, Insect ; Larva/cytology/growth & development ; Male ; Metamorphosis, Biological ; Molecular Sequence Data ; Mutation ; Ribosomal Protein S6 Kinases/genetics/*metabolism ; Wings, Animal/*cytology/growth & development
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    Drosophila egg-laying site selection as a system to study simple decision-making processes (2008)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2008-03-22
    Description: The ability to select a better option from multiple acceptable ones is important for animals to optimize their resources. The mechanisms that underlie such decision-making processes are not well understood. We found that selection of egg-laying site in Drosophila melanogaster is a suitable system to probe the neural circuit that governs simple decision-making processes. First, Drosophila females pursue active probing of the environment before depositing each egg, apparently to evaluate site quality for every egg. Second, Drosophila females can either accept or reject a sucrose-containing medium, depending on the context. Last, communication of the "acceptability" of the sucrose-containing medium as an egg-laying option to the reproductive system depends on the function of a group of insulin-like peptide 7 (ILP7)-producing neurons. These findings suggest that selection of egg-laying site involves a simple decision-making process and provide an entry point toward a systematic dissection of this process.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2581776/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2581776/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yang, Chung-Hui -- Belawat, Priyanka -- Hafen, Ernst -- Jan, Lily Y -- Jan, Yuh-Nung -- R01 MH084234/MH/NIMH NIH HHS/ -- R01 NS040929/NS/NINDS NIH HHS/ -- R01 NS040929-08/NS/NINDS NIH HHS/ -- R01 NS047200-04/NS/NINDS NIH HHS/ -- R01 NS40929/NS/NINDS NIH HHS/ -- R37 NS040929/NS/NINDS NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2008 Mar 21;319(5870):1679-83. doi: 10.1126/science.1151842.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Physiology, Biochemistry, and Biophysics, University of California at San Francisco, San Francisco, CA 94143-0725, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18356529" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Behavior, Animal ; *Decision Making ; Drosophila Proteins/metabolism ; *Drosophila melanogaster/physiology ; Female ; *Models, Animal ; Neurons/*physiology ; Neuropeptides/metabolism ; *Oviposition
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    Common and distinct roles of DFos and DJun during Drosophila development (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-10-24
    Description: The Drosophila homolog of c-Jun regulates epithelial cell shape changes during the process of dorsal closure in mid-embryogenesis. Here, mutations in the DFos gene are described. In dorsal closure, DFos cooperates with DJun by regulating the expression of dpp; Dpp acts as a relay signal that triggers cell shape changes and DFos expression in neighboring cells. In addition to the joint requirement of DFos and DJun during dorsal closure, DFos functions independently of DJun during early stages of embryogenesis. These findings demonstrate common and distinct roles of DFos and DJun during embryogenesis and suggest a conserved link between AP-1 (activating protein-1) and TGF-beta (transforming growth factor-beta) signaling during epithelial cell shape changes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Riesgo-Escovar, J R -- Hafen, E -- New York, N.Y. -- Science. 1997 Oct 24;278(5338):669-72.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Zoologisches Institut, Universitat Zurich, Winterthurerstrasse 190, CH-8057 Zurich, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9381174" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Size ; Dimerization ; Drosophila/*embryology/genetics/metabolism ; *Drosophila Proteins ; Ectoderm/metabolism ; Endoderm/metabolism ; Epithelial Cells/cytology/metabolism ; Gene Expression Regulation, Developmental ; Genes, Insect ; Genes, fos ; Genes, jun ; Homeodomain Proteins/genetics ; Insect Proteins/genetics/physiology ; *JNK Mitogen-Activated Protein Kinases ; MAP Kinase Kinase 4 ; Metamorphosis, Biological ; *Mitogen-Activated Protein Kinase Kinases ; Mutation ; Peptidyl-Dipeptidase A/genetics ; Phenotype ; Point Mutation ; Protein Kinases/genetics/metabolism ; Proto-Oncogene Proteins c-fos/*physiology ; Proto-Oncogene Proteins c-jun/*physiology ; Signal Transduction ; Transcription Factor AP-1/metabolism ; Transforming Growth Factor beta/genetics/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
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    Long-lived Drosophila with overexpressed dFOXO in adult fat body (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-06-12
    Description: Reduced activity of the insulin/insulin-like growth factor signaling (IIS) pathway increases life-span in diverse organisms. We investigated the timing of the effect of reduced IIS on life-span and the role of a potential target tissue, the fat body. We overexpressed dFOXO, a downstream effector of IIS, in the adult Drosophila fat body, which increased life-span and reduced fecundity of females but had no effect on male life-span. The role of FOXO transcription factors and the adipose tissue are therefore evolutionarily conserved in the regulation of aging, and reduction of IIS in the adult is sufficient to mediate its effects on life-span and fecundity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Giannakou, Maria E -- Goss, Martin -- Junger, Martin A -- Hafen, Ernst -- Leevers, Sally J -- Partridge, Linda -- SF19106/Biotechnology and Biological Sciences Research Council/United Kingdom -- New York, N.Y. -- Science. 2004 Jul 16;305(5682):361. Epub 2004 Jun 10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University College London, Darwin Building, Gower Street, London WC1E 6BT, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15192154" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Genetically Modified ; Drosophila Proteins/genetics/*physiology ; Drosophila melanogaster/genetics/*physiology ; Fat Body/*metabolism ; Female ; Fertility ; Forkhead Transcription Factors ; Gene Expression ; *Longevity ; Male ; Transcription Factors/genetics/*physiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
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    Living with lethal PIP3 levels: viability of flies lacking PTEN restored by a PH domain mutation in Akt/PKB (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-03-02
    Description: The phosphoinositide phosphatase PTEN is mutated in many human cancers. Although the role of PTEN has been studied extensively, the relative contributions of its numerous potential downstream effectors to deregulated growth and tumorigenesis remain uncertain. We provide genetic evidence in Drosophila melanogaster for the paramount importance of the protein kinase Akt [also called protein kinase B (PKB)] in mediating the effects of increased phosphatidylinositol 3,4,5-trisphosphate (PIP3) concentrations that are caused by the loss of PTEN function. A mutation in the pleckstrin homology (PH) domain of Akt that reduces its affinity for PIP3 sufficed to rescue the lethality of flies devoid of PTEN activity. Thus, Akt appears to be the only critical target activated by increased PIP3 concentrations in Drosophila.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stocker, Hugo -- Andjelkovic, Mirjana -- Oldham, Sean -- Laffargue, Muriel -- Wymann, Matthias P -- Hemmings, Brian A -- Hafen, Ernst -- New York, N.Y. -- Science. 2002 Mar 15;295(5562):2088-91. Epub 2002 Feb 28.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Zoologisches Institut der Universitat Zurich, Winterthurerstrasse 190, CH-8057 Zurich, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11872800" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Substitution ; Animals ; Cell Line ; Cell Membrane/enzymology ; Drosophila Proteins/chemistry/genetics/metabolism ; Drosophila melanogaster/genetics/*physiology ; Eye/growth & development ; Female ; Genes, Insect ; Humans ; Insulin/pharmacology ; Male ; Mutation ; PTEN Phosphohydrolase ; Phenotype ; Phosphatidylinositol 4,5-Diphosphate/metabolism ; Phosphatidylinositol Phosphates/*metabolism ; Phosphoric Monoester Hydrolases/*genetics/*physiology ; Photoreceptor Cells, Invertebrate/growth & development ; Protein Structure, Tertiary ; Protein-Serine-Threonine Kinases/chemistry/*genetics/metabolism ; Proto-Oncogene Proteins/chemistry/*genetics/metabolism ; Proto-Oncogene Proteins c-akt ; Transfection ; Tumor Suppressor Proteins/*genetics/*physiology ; Vanadates/pharmacology
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
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    Dietary restriction in long-lived dwarf flies (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-04-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Clancy, David J -- Gems, David -- Hafen, Ernst -- Leevers, Sally J -- Partridge, Linda -- SF19106/Biotechnology and Biological Sciences Research Council/United Kingdom -- New York, N.Y. -- Science. 2002 Apr 12;296(5566):319.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University College London, Gower Street, London WC1E 6BT, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11951037" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Body Constitution ; *Carrier Proteins ; Diet ; Drosophila Proteins/genetics/*physiology ; Drosophila melanogaster/genetics/*physiology ; *Energy Intake ; Female ; Genes, Insect ; Insulin Receptor Substrate Proteins ; *Intracellular Signaling Peptides and Proteins ; Longevity/*physiology ; Mutation ; Receptor, Insulin/physiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 9
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    Sending and receiving the hedgehog signal: control by the Drosophila Gli protein Cubitus interruptus (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-06-14
    Description: Drosophila limb development is organized by interactions between anterior and posterior compartment cells. Posterior cells continuously express and require engrailed (en) and secrete Hedgehog (Hh) protein. Anterior cells express the zinc-finger protein Cubitus interruptus (Ci). It is now shown that anterior cells lacking ci express hh and adopt posterior properties without expressing en. Increased levels of Ci can induce the expression of the Hh target gene decapentaplegic (dpp) in a Hh-independent manner. Thus, expression of Ci in anterior cells controls limb development (i) by restricting hh secretion to posterior cells and (ii) by conferring competence to respond to Hh by mediating the transduction of this signal.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dominguez, M -- Brunner, M -- Hafen, E -- Basler, K -- New York, N.Y. -- Science. 1996 Jun 14;272(5268):1621-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Zoologisches Institut, Universitat Zurich, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8658135" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; DNA-Binding Proteins/genetics/*physiology ; Drosophila/embryology/genetics ; *Drosophila Proteins ; *Embryonic Induction ; Female ; Gene Expression Regulation, Developmental ; Hedgehog Proteins ; Insect Hormones/genetics/physiology ; Male ; Membrane Proteins/genetics/physiology ; Models, Biological ; Mutagenesis ; Proteins/*physiology ; Receptors, Cell Surface ; *Signal Transduction ; Transcription Factors ; Zinc Fingers/genetics/*physiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
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    Ubiquitous expression of sevenless: position-dependent specification of cell fate (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-02-17
    Description: Specification of cell fate in the compound eye of Drosophila appears to be controlled entirely by cell interactions. The sevenless gene is required for the correct determination of one of the eight photoreceptor cells (R7) in each ommatidium. It encodes a transmembrane protein with a tyrosine kinase domain and is expressed transiently on a subpopulation of ommatidial precursor cells including the R7 precursors. It is shown here that heat shock-induced indiscriminate expression of a sevenless complementary DNA throughout development can correctly specify R7 cell identity without affecting the development of other cells. Furthermore, discontinuous supply of sevenless protein during eye development leads to the formation of mosaic eyes containing stripes of sevenless+ and sevenless- ommatidia, suggesting that R7 cell fate can be specified only within a relatively short period during ommatidial assembly. These results support the hypothesis that the specification of cell fate by position depends on the interaction of a localized signal with a receptor present on many undifferentiated cells, and that the mere presence of the receptor alone is not sufficient to specify cell fate.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Basler, K -- Hafen, E -- New York, N.Y. -- Science. 1989 Feb 17;243(4893):931-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Zoologisches Institut, Universitat Zurich, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2493159" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Communication ; Drosophila melanogaster/anatomy & histology/*genetics ; Eye/anatomy & histology/metabolism ; *Genes ; Heat-Shock Proteins/genetics ; Mutation ; Promoter Regions, Genetic ; Protein-Tyrosine Kinases/genetics ; RNA, Messenger/genetics
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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