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  • 1
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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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  • 2
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    Beta-arrestin 2 mediates endocytosis of type III TGF-beta receptor and down-regulation of its signaling (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-09-06
    Description: beta-Arrestins bind to activated seven transmembrane-spanning (7TMS) receptors (G protein-coupled receptors) after the receptors are phosphorylated by G protein-coupled receptor kinases (GRKs), thereby regulating their signaling and internalization. Here, we demonstrate an unexpected and analogous role of beta-arrestin 2 (betaarr2) for the single transmembrane-spanning type III transforming growth factor-beta (TGF-beta) receptor (TbetaRIII, also referred to as betaglycan). Binding of betaarr2 to TbetaRIII was also triggered by phosphorylation of the receptor on its cytoplasmic domain (likely at threonine 841). However, such phosphorylation was mediated by the type II TGF-beta receptor (TbetaRII), which is itself a kinase, rather than by a GRK. Association with betaarr2 led to internalization of both receptors and down-regulation of TGF-beta signaling. Thus, the regulatory actions of beta-arrestins are broader than previously appreciated, extending to the TGF-beta receptor family as well.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, Wei -- Kirkbride, Kellye C -- How, Tam -- Nelson, Christopher D -- Mo, Jinyao -- Frederick, Joshua P -- Wang, Xiao-Fan -- Lefkowitz, Robert J -- Blobe, Gerard C -- CA 75368/CA/NCI NIH HHS/ -- CA 91816/CA/NCI NIH HHS/ -- HL 16037/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 2003 Sep 5;301(5638):1394-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Duke University Medical Center, Departments of Medicine and Biochemistry, Durham, NC 27710, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12958365" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Arrestins/genetics/*metabolism ; Cell Line ; Cell Membrane/metabolism ; Cytoplasm/metabolism ; Down-Regulation ; *Endocytosis ; Humans ; Keratinocytes/metabolism ; Mice ; Mice, Knockout ; Molecular Sequence Data ; Mutagenesis ; Phosphorylation ; Protein Structure, Tertiary ; Protein-Serine-Threonine Kinases ; Proteoglycans/chemistry/genetics/*metabolism ; RNA, Small Interfering ; Receptors, Transforming Growth Factor beta/chemistry/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; *Signal Transduction ; Transfection ; Transforming Growth Factor beta ; Transforming Growth Factor beta1
    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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  • 3
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    Targeting of diacylglycerol degradation to M1 muscarinic receptors by beta-arrestins (2007)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2007-02-03
    Description: Seven-transmembrane receptor (7TMR) signaling is transduced by second messengers such as diacylglycerol (DAG) generated in response to the heterotrimeric guanine nucleotide-binding protein Gq and is terminated by receptor desensitization and degradation of the second messengers. We show that beta-arrestins coordinate both processes for the Gq-coupled M1 muscarinic receptor. beta-Arrestins physically interact with diacylglycerol kinases (DGKs), enzymes that degrade DAG. Moreover, beta-arrestins are essential for conversion of DAG to phosphatidic acid after agonist stimulation, and this activity requires recruitment of the beta-arrestin-DGK complex to activated 7TMRs. The dual function of beta-arrestins, limiting production of diacylglycerol (by receptor desensitization) while enhancing its rate of degradation, is analogous to their ability to recruit adenosine 3',5'-monophosphate phosphodiesterases to Gs-coupled beta2-adrenergic receptors. Thus, beta-arrestins can serve similar regulatory functions for disparate classes of 7TMRs through structurally dissimilar enzymes that degrade chemically distinct second messengers.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nelson, Christopher D -- Perry, Stephen J -- Regier, Debra S -- Prescott, Stephen M -- Topham, Matthew K -- Lefkowitz, Robert J -- CA95463/CA/NCI NIH HHS/ -- HL16037/HL/NHLBI NIH HHS/ -- HL70631/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 2007 Feb 2;315(5812):663-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of 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/17272726" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arrestins/*metabolism ; COS Cells ; Carbachol/pharmacology ; Cell Line ; Cercopithecus aethiops ; Diacylglycerol Kinase/genetics/*metabolism ; Diglycerides/*metabolism ; Humans ; Mutation ; Phosphatidic Acids/metabolism ; Protein Binding ; RNA, Small Interfering ; Receptor, Muscarinic M1/*metabolism ; Recombinant Fusion Proteins/metabolism ; Second Messenger Systems ; *Signal Transduction ; 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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