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  • 1
    Electronic Resource
    Electronic Resource
    Cocaine addiction therapy—Are we partially there? (1999)
    [s.l.] : Nature America Inc.
    Nature medicine 5 (1999), S. 993-995 
    Details
    ISSN: 1546-170X
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] A recent study suggests that the dopamine D3 receptor partial agonist BP 897 prevents cocaine-seeking behavior in rats, and this may lead to new approaches to study and treat drug ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/12429
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    Paper (German National Licenses)
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  • 2
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    A rapid and affordable screening platform for membrane protein trafficking (2015)
    BioMed Central
    Details
    Publication Date: 2015-12-19
    Description: Membrane proteins regulate a diversity of physiological processes and are the most successful class of targets in drug discovery. However, the number of targets adequately explored in chemical space and the li...
    Electronic ISSN: 1741-7007
    Topics: Biology
    Published by BioMed Central
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  • 3
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    Phenotypic Regulation of the Sphingosine 1-Phosphate Receptor Miles Apart by G Protein-Coupled Receptor Kinase 2 (2015)
    American Chemical Society (ACS)
    Details
    Publication Date: 2015-01-16
    Description: Biochemistry DOI: 10.1021/bi501061h
    Print ISSN: 0006-2960
    Electronic ISSN: 1520-4995
    Topics: Biology , Chemistry and Pharmacology
    Published by American Chemical Society (ACS)
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  • 4
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    Role of the sphingosine-1-phosphate receptor EDG-1 in PDGF-induced cell motility (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-03-07
    Description: EDG-1 is a heterotrimeric guanine nucleotide binding protein-coupled receptor (GPCR) for sphingosine-1-phosphate (SPP). Cell migration toward platelet-derived growth factor (PDGF), which stimulates sphingosine kinase and increases intracellular SPP, was dependent on expression of EDG-1. Deletion of edg-1 or inhibition of sphingosine kinase suppressed chemotaxis toward PDGF and also activation of the small guanosine triphosphatase Rac, which is essential for protrusion of lamellipodia and forward movement. Moreover, PDGF activated EDG-1, as measured by translocation of beta-arrestin and phosphorylation of EDG-1. Our results reveal a role for receptor cross-communication in which activation of a GPCR by a receptor tyrosine kinase is critical for cell motility.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hobson, J P -- Rosenfeldt, H M -- Barak, L S -- Olivera, A -- Poulton, S -- Caron, M G -- Milstien, S -- Spiegel, S -- CA61774/CA/NCI NIH HHS/ -- GM43880/GM/NIGMS NIH HHS/ -- HL-61365/HL/NHLBI NIH HHS/ -- NS19576/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2001 Mar 2;291(5509):1800-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, Georgetown University Medical Center, Washington, DC 20007, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11230698" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arrestins/metabolism ; Cell Line ; Cell Membrane/metabolism ; Cells, Cultured ; *Chemotaxis/drug effects ; Gene Deletion ; Humans ; Immediate-Early Proteins/genetics/*metabolism ; *Lysophospholipids ; Mice ; Muscle, Smooth, Vascular/cytology/metabolism ; Phosphorylation ; Phosphotransferases (Alcohol Group Acceptor)/antagonists & inhibitors/metabolism ; Platelet-Derived Growth Factor/metabolism/*pharmacology ; Proto-Oncogene Proteins c-sis ; Receptor Cross-Talk ; *Receptors, Cell Surface ; *Receptors, G-Protein-Coupled ; Receptors, Lysophospholipid ; Receptors, Platelet-Derived Growth Factor/metabolism ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; Sphingosine/*analogs & derivatives/*metabolism/pharmacology ; Transfection
    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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  • 5
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    Dishevelled 2 recruits beta-arrestin 2 to mediate Wnt5A-stimulated endocytosis of Frizzled 4 (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-09-06
    Description: Wnt proteins, regulators of development in many organisms, bind to seven transmembrane-spanning (7TMS) receptors called frizzleds, thereby recruiting the cytoplasmic molecule dishevelled (Dvl) to the plasma membrane.Frizzled-mediated endocytosis of Wg (a Drosophila Wnt protein) and lysosomal degradation may regulate the formation of morphogen gradients. Endocytosis of Frizzled 4 (Fz4) in human embryonic kidney 293 cells was dependent on added Wnt5A protein and was accomplished by the multifunctional adaptor protein beta-arrestin 2 (betaarr2), which was recruited to Fz4 by binding to phosphorylated Dvl2. These findings provide a previously unrecognized mechanism for receptor recruitment of beta-arrestin and demonstrate that Dvl plays an important role in the endocytosis of frizzled, as well as in promoting signaling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, Wei -- ten Berge, Derk -- Brown, Jeff -- Ahn, Seungkirl -- Hu, Liaoyuan A -- Miller, William E -- Caron, Marc G -- Barak, Larry S -- Nusse, Roel -- Lefkowitz, Robert J -- HL 16037/HL/NHLBI NIH HHS/ -- HL 61365/HL/NHLBI NIH HHS/ -- NS 19576/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2003 Sep 5;301(5638):1391-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Departments of Medicine and Biochemistry, Duke University Medical Center, Durham, NC 27710, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12958364" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing ; Animals ; Arrestins/genetics/*metabolism ; Cell Line ; Cell Membrane/metabolism ; Clathrin/metabolism ; Cytoplasm/metabolism ; *Endocytosis ; Frizzled Receptors ; Humans ; Mice ; Phosphoproteins/metabolism ; Phosphorylation ; Protein Kinase C/antagonists & inhibitors/metabolism ; Proteins/genetics/*metabolism ; Proto-Oncogene Proteins/*metabolism/pharmacology ; RNA, Small Interfering ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; Wnt 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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  • 6
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    Beta-arrestin 2 regulates zebrafish development through the hedgehog signaling pathway (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-12-25
    Description: beta-arrestins are multifunctional proteins that act as scaffolds and transducers of intracellular signals from heptahelical transmembrane-spanning receptors (7TMR). Hedgehog (Hh) signaling, which uses the putative 7TMR, Smoothened, is established as a fundamental pathway in development, and unregulated Hh signaling is associated with certain malignancies. Here, we show that the functional knockdown of beta-arrestin 2 in zebrafish embryos recapitulates the many phenotypes of Hh pathway mutants. Expression of wild-type beta-arrestin 2, or constitutive activation of the Hh pathway downstream of Smoothened, rescues the phenotypes caused by beta-arrestin 2 deficiency. These results suggest that a functional interaction between beta-arrestin 2 and Smoothened may be critical to regulate Hh signaling in zebrafish development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wilbanks, Alyson M -- Fralish, Gregory B -- Kirby, Margaret L -- Barak, Larry S -- Li, Yin-Xiong -- Caron, Marc G -- GM069086-01/GM/NIGMS NIH HHS/ -- HL36059/HL/NHLBI NIH HHS/ -- HL61365/HL/NHLBI NIH HHS/ -- NS19576/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2004 Dec 24;306(5705):2264-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Center for Models of Human Disease, Institute for Genome Science and Policy, Duke University Medical Center, Durham, NC 27710, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15618520" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arrestins/genetics/*physiology ; Cell Differentiation ; Cyclic AMP-Dependent Protein Kinases/genetics/metabolism ; Embryo, Nonmammalian/metabolism ; Gene Expression Regulation, Developmental ; Hedgehog Proteins ; Homeodomain Proteins/genetics/metabolism ; In Situ Hybridization ; Membrane Proteins/genetics/metabolism ; Muscle Cells/cytology ; Muscle Fibers, Skeletal/cytology ; Mutation ; Phenotype ; Receptors, Cell Surface ; Receptors, G-Protein-Coupled/genetics/physiology ; Repressor Proteins/genetics/metabolism ; *Signal Transduction ; Trans-Activators/genetics/*metabolism ; Transcription Factors/genetics/metabolism ; Zebrafish/*embryology/genetics/*metabolism ; Zebrafish Proteins/genetics/metabolism/*physiology
    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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  • 7
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    Activity-dependent internalization of smoothened mediated by beta-arrestin 2 and GRK2 (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-12-25
    Description: Binding of Sonic Hedgehog (Shh) to Patched (Ptc) relieves the latter's tonic inhibition of Smoothened (Smo), a receptor that spans the cell membrane seven times. This initiates signaling which, by unknown mechanisms, regulates vertebrate developmental processes. We find that two molecules interact with mammalian Smo in an activation-dependent manner: G protein-coupled receptor kinase 2 (GRK2) leads to phosphorylation of Smo, and beta-arrestin 2 fused to green fluorescent protein interacts with Smo. These two processes promote endocytosis of Smo in clathrin-coated pits. Ptc inhibits association of beta-arrestin 2 with Smo, and this inhibition is relieved in cells treated with Shh. A Smo agonist stimulated and a Smo antagonist (cyclopamine) inhibited both phosphorylation of Smo by GRK2 and interaction of beta-arrestin 2 with Smo. beta-Arrestin 2 and GRK2 are thus potential mediators of signaling by activated Smo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, Wei -- Ren, Xiu-Rong -- Nelson, Christopher D -- Barak, Larry S -- Chen, James K -- Beachy, Philip A -- de Sauvage, Frederic -- Lefkowitz, Robert J -- New York, N.Y. -- Science. 2004 Dec 24;306(5705):2257-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, Duke University Medical Center, Durham, NC 27710, USA. w.chen@duke.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15618519" target="_blank"〉PubMed〈/a〉
    Keywords: Arrestins/*metabolism ; Cell Line ; Cell Membrane/*metabolism ; Clathrin/metabolism ; Coated Pits, Cell-Membrane/metabolism ; Cyclic AMP-Dependent Protein Kinases/*metabolism ; Cyclohexylamines/pharmacology ; Cytosol/metabolism ; Dynamins/metabolism ; Endocytosis ; Hedgehog Proteins ; Humans ; Membrane Proteins/metabolism ; Phosphorylation ; Receptors, Cell Surface ; Receptors, G-Protein-Coupled/*metabolism ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; Thiophenes/pharmacology ; Trans-Activators/metabolism ; Transfection ; Veratrum Alkaloids/pharmacology ; beta-Adrenergic Receptor Kinases
    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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  • 8
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    Role of beta-arrestin in mediating agonist-promoted G protein-coupled receptor internalization (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-01-19
    Description: beta-Arrestins are proteins that bind phosphorylated heterotrimeric GTP-binding protein (G protein)-coupled receptors (GPCRs) and contribute to the desensitization of GPCRs by uncoupling the signal transduction process. Resensitization of GPCR responsiveness involves agonist-mediated receptor sequestration. Overexpression of beta-arrestins in human embryonic kidney cells rescued the sequestration of beta 2-adrenergic receptor (beta 2AR) mutants defective in their ability to sequester, an effect enhanced by simultaneous overexpression of beta-adrenergic receptor kinase 1. Wild-type beta 2AR sequestration was inhibited by the overexpression of two beta-arrestin mutants. These findings suggest that beta-arrestins play an integral role in GPCR internalization and thus serve a dual role in the regulation of GPCR function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ferguson, S S -- Downey, W E 3rd -- Colapietro, A M -- Barak, L S -- Menard, L -- Caron, M G -- NS 19576/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1996 Jan 19;271(5247):363-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute Laboratory, Duke University Medical Center, Durham, NC 27710, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8553074" target="_blank"〉PubMed〈/a〉
    Keywords: Adrenergic beta-Agonists/*pharmacology ; Antigens/genetics/*physiology ; *Arrestins ; Cell Line ; Cyclic AMP-Dependent Protein Kinases/genetics/*metabolism ; DNA, Complementary ; Eye Proteins/genetics/*physiology ; GTP-Binding Proteins/*metabolism ; Humans ; Isoproterenol/pharmacology ; Mutation ; Phosphorylation ; Point Mutation ; Receptors, Adrenergic, beta-2/genetics/*metabolism ; Transfection ; beta-Adrenergic Receptor Kinases
    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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  • 9
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    An antiviral soluble form of the LDL receptor induced by interferon (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-10-08
    Description: Interferons, which induce several intracellular antiviral proteins, also induce an extracellular soluble protein that inhibits vesicular stomatitis virus (VSV) infection. This 28-kilodalton soluble protein was purified to homogeneity and identified by protein sequencing as the ligand-binding domain of the human 160-kilodalton low density lipoprotein receptor (LDLR). The existence of an antiviral soluble LDLR was confirmed by immunoaffinity chromatography with monoclonal antibody to LDLR. This soluble receptor mediates most of the interferon-triggered antiviral activity against VSV, apparently by interfering with virus assembly or budding, and not by inhibiting virus attachment to cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fischer, D G -- Tal, N -- Novick, D -- Barak, S -- Rubinstein, M -- New York, N.Y. -- Science. 1993 Oct 8;262(5131):250-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Genetics and Virology, Weizmann Institute of Science, Rehovot, Israel.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8211145" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antiviral Agents/*biosynthesis/chemistry/isolation & purification ; Cell Line ; Cells, Cultured ; Chromatography, Affinity ; Culture Media, Serum-Free ; Cytopathogenic Effect, Viral ; HeLa Cells ; Humans ; Interferon-beta/pharmacology ; Interferon-gamma/*pharmacology ; Molecular Sequence Data ; Molecular Weight ; Receptors, LDL/*biosynthesis/chemistry/isolation & purification ; Solubility ; Vesicular stomatitis Indiana virus/growth & development
    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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  • 10
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    Novel Adamantyl Cannabinoids as CB1 Receptor Probes (2013)
    American Chemical Society (ACS)
    Details
    Publication Date: 2013-05-15
    Description: Journal of Medicinal Chemistry DOI: 10.1021/jm4000775
    Topics: Chemistry and Pharmacology
    Published by American Chemical Society (ACS)
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