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  • 1
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    Phosphoinositide signalling links O-GlcNAc transferase to insulin resistance (2008)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2008-02-22
    Description: Glucose flux through the hexosamine biosynthetic pathway leads to the post-translational modification of cytoplasmic and nuclear proteins by O-linked beta-N-acetylglucosamine (O-GlcNAc). This tandem system serves as a nutrient sensor to couple systemic metabolic status to cellular regulation of signal transduction, transcription, and protein degradation. Here we show that O-GlcNAc transferase (OGT) harbours a previously unrecognized type of phosphoinositide-binding domain. After induction with insulin, phosphatidylinositol 3,4,5-trisphosphate recruits OGT from the nucleus to the plasma membrane, where the enzyme catalyses dynamic modification of the insulin signalling pathway by O-GlcNAc. This results in the alteration in phosphorylation of key signalling molecules and the attenuation of insulin signal transduction. Hepatic overexpression of OGT impairs the expression of insulin-responsive genes and causes insulin resistance and dyslipidaemia. These findings identify a molecular mechanism by which nutritional cues regulate insulin signalling through O-GlcNAc, and underscore the contribution of this modification to the aetiology of insulin resistance and type 2 diabetes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yang, Xiaoyong -- Ongusaha, Pat P -- Miles, Philip D -- Havstad, Joyce C -- Zhang, Fengxue -- So, W Venus -- Kudlow, Jeffrey E -- Michell, Robert H -- Olefsky, Jerrold M -- Field, Seth J -- Evans, Ronald M -- P30 CA014195/CA/NCI NIH HHS/ -- Howard Hughes Medical Institute/ -- England -- Nature. 2008 Feb 21;451(7181):964-9. doi: 10.1038/nature06668.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Gene Expression Laboratory, The Salk Institute for Biological Studies, La Jolla, California 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18288188" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylglucosamine/metabolism/pharmacology ; Animals ; COS Cells ; Cell Membrane/metabolism ; Cercopithecus aethiops ; Insulin/pharmacology ; Insulin Resistance/*physiology ; Lipid Metabolism ; Liver/enzymology/metabolism ; Male ; Mice ; Mice, Inbred C57BL ; N-Acetylglucosaminyltransferases/chemistry/genetics/*metabolism ; Phosphatidylinositol Phosphates/metabolism ; Phosphatidylinositols/*metabolism ; Phosphorylation/drug effects ; Protein Structure, Tertiary ; Protein Transport ; *Second Messenger Systems/drug effects
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 2
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    Inhibition of phosphatases and increased Ca2+ channel activity by inositol hexakisphosphate (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-10-23
    Description: Inositol hexakisphosphate (InsP6), the dominant inositol phosphate in insulin-secreting pancreatic beta cells, inhibited the serine-threonine protein phosphatases type 1, type 2A, and type 3 in a concentration-dependent manner. The activity of voltage-gated L-type calcium channels is increased in cells treated with inhibitors of serine-threonine protein phosphatases. Thus, the increased calcium channel activity obtained in the presence of InsP6 might result from the inhibition of phosphatase activity. Glucose elicited a transient increase in InsP6 concentration, which indicates that this inositol polyphosphate may modulate calcium influx over the plasma membrane and serve as a signal in the pancreatic beta cell stimulus-secretion coupling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Larsson, O -- Barker, C J -- Sjoholm, A -- Carlqvist, H -- Michell, R H -- Bertorello, A -- Nilsson, T -- Honkanen, R E -- Mayr, G W -- Zwiller, J -- Berggren, P O -- New York, N.Y. -- Science. 1997 Oct 17;278(5337):471-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Rolf Luft Center for Diabetes Research, Department of Molecular Medicine, Karolinska Institute, S-171 76 Stockholm, Sweden.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9334307" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/metabolism ; Calcium Channels/drug effects/*metabolism ; Cell Membrane/metabolism ; Cricetinae ; Dose-Response Relationship, Drug ; Glucose/pharmacology ; Inositol/pharmacology ; Inositol Phosphates/pharmacology ; Ion Channel Gating ; Islets of Langerhans/drug effects/*metabolism ; Patch-Clamp Techniques ; Phosphoprotein Phosphatases/*antagonists & inhibitors ; Phytic Acid/*pharmacology ; Tumor Cells, Cultured
    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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    The buck stops with government (1990)
    Springer Nature
    Details
    Publication Date: 1990-11-01
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Springer Nature
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  • 4
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    ITP nomenclature (1984)
    Springer Nature
    Details
    Publication Date: 1984-01-01
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Springer Nature
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  • 5
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    Receptors and recognition (1978)
    Springer Nature
    Details
    Publication Date: 1978-11-01
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Springer Nature
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  • 6
    Electronic Resource
    Electronic Resource
    Receptors and recognition (1978)
    [s.l.] : Nature Publishing Group
    Nature 276 (1978), S. 540-540 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] PREVIOUS volumes in this series have contained four or five articles, but this one contains only three, albeit rather longer, contributions. "Relationships in the structure and function of receptors for glycoprotein hormones, bacterial toxins and interferon" by L. D. Kohn is a contribution central ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/276540a0
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  • 7
    Electronic Resource
    Electronic Resource
    ITP nomenclature (1984)
    [s.l.] : Nature Publishing Group
    Nature 307 (1984), S. 116-116 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] SIR - The interesting recent letter Nature (3 November, 1983 p.67-69) and News and Views article (3 November, p. 16-17) on the possible second messenger function of inositol 1,4,5-trisphosphate may presage a surge of interest in the function and metabolism of inositol phosphates. It would therefore ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/307116b0
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  • 8
    Electronic Resource
    Electronic Resource
    The buck stops with government (1990)
    [s.l.] : Nature Publishing Group
    Nature 348 (1990), S. 190-190 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] SIR-The recent debate on the closure of several major research groups by the MRC has mainly focused on the way in which the council has taken these decisions. I have recently been on one of the MRC research boards, and from 1980 to 1990 I chaired one of the MRC committees that rank applications for ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/348190a0
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