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  • 1
    Publication Date: 2002-10-05
    Description: The African malaria mosquito, Anopheles gambiae, is specialized for rapid completion of development and reproduction. A vertebrate blood meal is required for egg production, and multiple feedings subsequently allow transmission of malaria parasites, Plasmodium spp. Regulatory peptides from 35 genes annotated from the A. gambiae genome likely coordinate these and other physiological processes. Plasmodium parasites may affect actions of newly identified insulin-like peptides, which coordinate growth and reproduction of its vector, A. gambiae, as in Drosophila melanogaster, Caenorhabditis elegans, and mammals. This genomic information provides a basis to expand understanding of hematophagy and pathogen transmission in this mosquito.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Riehle, Michael A -- Garczynski, Stephen F -- Crim, Joe W -- Hill, Catherine A -- Brown, Mark R -- AI33108/AI/NIAID NIH HHS/ -- R01 AI033108/AI/NIAID NIH HHS/ -- U01 AI48846/AI/NIAID NIH HHS/ -- U01 AI50687/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2002 Oct 4;298(5591):172-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Entomology, University of Georgia, Athens, GA 30602, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12364794" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Anopheles/chemistry/genetics/parasitology/*physiology ; Blood ; Computational Biology ; Cues ; Ecdysteroids/secretion ; Feeding Behavior ; Female ; Genes, Insect ; Homeostasis ; Insect Hormones/chemistry/genetics/*metabolism ; Insect Proteins/chemistry/genetics/*metabolism ; Insulin/metabolism ; Molecular Sequence Data ; Molting ; Neuropeptides/chemistry/genetics/*metabolism ; Peptides/chemistry/genetics/*metabolism ; Plasmodium/physiology ; Signal Transduction ; Water-Electrolyte Balance
    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
    Publication Date: 2002-08-31
    Description: We exploited the high rate of homologous recombination shown by the chicken B cell line DT40 to inactivate the endogenous alleles for clathrin heavy chain and replace them with human clathrin complementary DNA under the control of a tetracycline-regulatable promoter. Clathrin repression perturbed the activities of Akt-mediated and mitogen-activated protein kinase-mediated signaling pathways and induced apoptosis; this finding suggests that in DT40 cells clathrin helps to maintain the integrity of antiapoptotic survival pathways. We also describe a variant cell line in which these signaling pathways were unaffected by clathrin down-regulation. This variant cell line did not undergo apoptosis in the absence of clathrin and was used to examine the effects of clathrin depletion on membrane-trafficking pathways. Receptor-mediated and fluid-phase endocytosis were both substantially inhibited, and transferrin-receptor recycling was modestly inhibited. Surprisingly, clathrin removal did not affect the morphology or biochemical composition of lysosomes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wettey, Frank R -- Hawkins, Steve F C -- Stewart, Abigail -- Luzio, J Paul -- Howard, Jonathan C -- Jackson, Antony P -- New York, N.Y. -- Science. 2002 Aug 30;297(5586):1521-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Cambridge, Building O, Downing Site, Tennis Court Road, Cambridge CB2 1QW, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12202821" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Apoptosis ; B-Lymphocytes/*metabolism/ultrastructure ; Cell Line ; Chickens ; Clathrin/biosynthesis/*genetics/physiology ; Clathrin Heavy Chains ; Down-Regulation ; Doxycycline/pharmacology ; Endocytosis/physiology ; *Gene Expression Regulation/drug effects ; Lysosomes/physiology ; Membrane Proteins/physiology ; Molecular Sequence Data ; 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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  • 3
    Publication Date: 2002-06-08
    Description: The site of induction of long-term potentiation (LTP) at mossy fiber-CA3 synapses in the hippocampus is unresolved, with data supporting both pre- and postsynaptic mechanisms. Here we report that mossy fiber LTP was reduced by perfusion of postsynaptic neurons with peptides and antibodies that interfere with binding of EphB receptor tyrosine kinases (EphRs) to the PDZ protein GRIP. Mossy fiber LTP was also reduced by extracellular application of soluble forms of B-ephrins, which are normally membrane-anchored presynaptic ligands for the EphB receptors. The application of soluble ligands for presynaptic ephrins increased basal excitatory transmission and occluded both tetanus and forskolin-induced synaptic potentiation. These findings suggest that PDZ interactions in the postsynaptic neuron and trans-synaptic interactions between postsynaptic EphB receptors and presynaptic B-ephrins are necessary for the induction of mossy fiber LTP.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Contractor, Anis -- Rogers, Cheryl -- Maron, Cornelia -- Henkemeyer, Mark -- Swanson, Geoffrey T -- Heinemann, Stephen F -- R01 MH066332/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 2002 Jun 7;296(5574):1864-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Neurobiology Laboratory, The Salk Institute for Biological Studies, 10010 North Torrey Pines Road, La Jolla, CA 92037, USA. contractor@salk.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12052960" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing ; Amino Acid Motifs ; Animals ; Carrier Proteins/metabolism ; Colforsin/pharmacology ; Cyclic AMP-Dependent Protein Kinases/metabolism ; Ephrin-B1 ; Excitatory Postsynaptic Potentials ; In Vitro Techniques ; Ligands ; *Long-Term Potentiation ; Membrane Proteins/*metabolism ; Mice ; Mossy Fibers, Hippocampal/*physiology ; Nerve Tissue Proteins/metabolism ; Patch-Clamp Techniques ; Peptide Fragments/metabolism ; Receptor Protein-Tyrosine Kinases/*metabolism ; Receptor, EphA7 ; Receptor, EphB2 ; Receptors, AMPA/metabolism ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; Synapses/*physiology ; Synaptic Transmission
    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
    Publication Date: 2003-05-17
    Description: Asymmetric divisions are crucial for generating cell diversity; they rely on coupling between polarity cues and spindle positioning, but how this coupling is achieved is poorly understood. In one-cell stage Caenorhabditis elegans embryos, polarity cues set by the PAR proteins mediate asymmetric spindle positioning by governing an imbalance of net pulling forces acting on spindle poles. We found that the GoLoco-containing proteins GPR-1 and GPR-2, as well as the Galpha subunits GOA-1 and GPA-16, were essential for generation of proper pulling forces. GPR-1/2 interacted with guanosine diphosphate-bound GOA-1 and were enriched on the posterior cortex in a par-3- and par-2-dependent manner. Thus, the extent of net pulling forces may depend on cortical Galpha activity, which is regulated by anterior-posterior polarity cues through GPR-1/2.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Colombo, Kelly -- Grill, Stephan W -- Kimple, Randall J -- Willard, Francis S -- Siderovski, David P -- Gonczy, Pierre -- GM62338/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2003 Jun 20;300(5627):1957-61. Epub 2003 May 15.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Swiss Institute for Experimental Cancer Research (ISREC), 1066 Epalinges/Lausanne, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12750478" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Genetically Modified ; Caenorhabditis elegans/cytology/*embryology/genetics/physiology ; Caenorhabditis elegans Proteins/genetics/*metabolism ; *Cell Division ; *Cell Polarity ; Cues ; GTP-Binding Proteins/genetics/metabolism ; Phenotype ; Protein Subunits/genetics/metabolism ; RNA Interference ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; Spindle Apparatus/*physiology/ultrastructure ; Two-Hybrid System Techniques
    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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