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  • Humans  (2)
  • American Association for the Advancement of Science (AAAS)  (2)
  • 2000-2004  (1)
  • 1995-1999  (1)
  • 1
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    Sphingosine-1-phosphate as a ligand for the G protein-coupled receptor EDG-1 (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-03-21
    Description: The sphingolipid metabolite sphingosine-1-phosphate (SPP) has been implicated as a second messenger in cell proliferation and survival. However, many of its biological effects are due to binding to unidentified receptors on the cell surface. SPP activated the heterotrimeric guanine nucleotide binding protein (G protein)-coupled orphan receptor EDG-1, originally cloned as Endothelial Differentiation Gene-1. EDG-1 bound SPP with high affinity (dissociation constant = 8.1 nM) and high specificity. Overexpression of EDG-1 induced exaggerated cell-cell aggregation, enhanced expression of cadherins, and formation of well-developed adherens junctions in a manner dependent on SPP and the small guanine nucleotide binding protein Rho.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, M J -- Van Brocklyn, J R -- Thangada, S -- Liu, C H -- Hand, A R -- Menzeleev, R -- Spiegel, S -- Hla, T -- DK45659/DK/NIDDK NIH HHS/ -- GM43880/GM/NIGMS NIH HHS/ -- HL49094/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1998 Mar 6;279(5356):1552-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, University of Connecticut School of Medicine, Farmington, CT 06030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9488656" target="_blank"〉PubMed〈/a〉
    Keywords: Cadherins/*biosynthesis ; *Cell Aggregation ; Cell Differentiation ; Cell Line ; Cloning, Molecular ; GTP-Binding Proteins/metabolism ; Gene Expression ; Genes, Immediate-Early ; Humans ; Immediate-Early Proteins/genetics/*metabolism ; Intercellular Junctions/*ultrastructure ; Ligands ; *Lysophospholipids ; Mitogen-Activated Protein Kinase 1/metabolism ; Morphogenesis ; Receptors, Cell Surface/genetics/*metabolism ; *Receptors, G-Protein-Coupled ; Receptors, Lysophospholipid ; Signal Transduction ; Sphingosine/*analogs & derivatives/metabolism ; Transfection ; rho GTP-Binding Proteins
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    Dissection of the mammalian midbody proteome reveals conserved cytokinesis mechanisms (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-05-29
    Description: Cytokinesis is the essential process that partitions cellular contents into daughter cells. To identify and characterize cytokinesis proteins rapidly, we used a functional proteomic and comparative genomic strategy. Midbodies were isolated from mammalian cells, proteins were identified by multidimensional protein identification technology (MudPIT), and protein function was assessed in Caenorhabditis elegans. Of 172 homologs disrupted by RNA interference, 58% displayed defects in cleavage furrow formation or completion, or germline cytokinesis. Functional dissection of the midbody demonstrated the importance of lipid rafts and vesicle trafficking pathways in cytokinesis, and the utilization of common membrane cytoskeletal components in diverse morphogenetic events in the cleavage furrow, the germline, and neurons.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3679889/" 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/PMC3679889/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Skop, Ahna R -- Liu, Hongbin -- Yates, John 3rd -- Meyer, Barbara J -- Heald, Rebecca -- F32 GM064159/GM/NIGMS NIH HHS/ -- F32 GM064159-01/GM/NIGMS NIH HHS/ -- F32 GM064159-02/GM/NIGMS NIH HHS/ -- F32 GM064159-03/GM/NIGMS NIH HHS/ -- F32 GM64159-01/GM/NIGMS NIH HHS/ -- P41 RR011823/RR/NCRR NIH HHS/ -- RR1823/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2004 Jul 2;305(5680):61-6. Epub 2004 May 27.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, CA 94720, USA. skop@wisc.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15166316" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; CHO Cells ; Caenorhabditis elegans/cytology/genetics/physiology ; Carrier Proteins/analysis/isolation & purification/physiology ; Cell Cycle/physiology ; *Cell Division ; Cell Fractionation ; Cell Membrane/physiology ; Computational Biology ; Cricetinae ; Cytoskeletal Proteins/analysis/isolation & purification/physiology ; Cytoskeleton/physiology ; Germ Cells/physiology ; HeLa Cells ; Humans ; Membrane Microdomains/physiology ; Morphogenesis ; Organelles/chemistry/*physiology ; Protein Transport ; Proteins/analysis/isolation & purification/*physiology ; Proteome/*analysis ; Proteomics ; Signal Transduction ; Spindle Apparatus/physiology/ultrastructure
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
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