Tyrosine phosphorylation of Phosphoinositide-dependent kinase-1 by the insulin receptor is necessary for insulin metabolic signaling. (Articolo in rivista)

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  • Tyrosine phosphorylation of Phosphoinositide-dependent kinase-1 by the insulin receptor is necessary for insulin metabolic signaling. (Articolo in rivista) (literal)
Anno
  • 2005-01-01T00:00:00+01:00 (literal)
Alternative label
  • Fiory F; Alberobello A. T.; Miele C.; Oriente F.; Esposito I.; Corbo V.; Ruvo M.; Tizzano B.; Rasmussen T.E.; Gammeltoft S.; Formisano P.; and Beguinot F. (2005)
    Tyrosine phosphorylation of Phosphoinositide-dependent kinase-1 by the insulin receptor is necessary for insulin metabolic signaling.
    in Molecular and cellular biology (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Fiory F; Alberobello A. T.; Miele C.; Oriente F.; Esposito I.; Corbo V.; Ruvo M.; Tizzano B.; Rasmussen T.E.; Gammeltoft S.; Formisano P.; and Beguinot F. (literal)
Pagina inizio
  • 10803 (literal)
Pagina fine
  • 10814 (literal)
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  • 25 (literal)
Rivista
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  • 24 (literal)
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  • Pubblicazione scientifica (literal)
Note
  • ISI Web of Science (WOS) (literal)
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  • Dipartimento di Biologia e Patologia Cellulare e Molecolare & Istituto di Endocrinologia ed Oncologia Sperimentale del CNR, Universita` degli Studi di Napoli Federico II, Naples, Italy; Istituto di Biostrutture e Bioimmagini del CNR, Naples, Italy; and Department of Clinical Biochemistry, Glostrup Hospital, DK 2600 Glostrup, Denmark (literal)
Titolo
  • Tyrosine phosphorylation of Phosphoinositide-dependent kinase-1 by the insulin receptor is necessary for insulin metabolic signaling. (literal)
Abstract
  • In L6 myoblasts, insulin receptors with deletion of the C-terminal 43 amino acids (IRƒ´43) exhibited normal autophosphorylation and IRS-1/2 tyrosine phosphorylation. The L6 cells expressing IRƒ´43 (L6IRƒ´43) also showed no insulin effect on glucose uptake and glycogen synthase, accompanied by a >80% decrease in insulin induction of 3-phosphoinositide-dependent protein kinase 1 (PDK-1) activity and tyrosine phosphorylation and of protein kinase B (PKB) phosphorylation at Thr308. Insulin induced the phosphatidylinositol 3 kinase-dependent copptn. of PDK-1 with wild-type IR (IRWT), but not IRƒ´43. Based on overlay blotting, PDK-1 directly bound IRWT, but not IRƒ´43. Insulin-activated IRWT, and not IRƒ´43, phosphorylated PDK-1 at tyrosines 9, 373, and 376. The IR C-terminal 43-amino-acid peptide (C-terminal peptide) inhibited in vitro PDK-1 tyrosine phosphorylation by the IR. Tyr„_Phe substitution prevented this inhibitory action. In the L6hIR cells, the C-terminal peptide copptd. with PDK-1 in an insulin-stimulated fashion. This peptide simultaneously impaired the insulin effect on PDK-1 copptn. with IRWT, on PDK-1 tyrosine phosphorylation, on PKB phosphorylation at Thr308, and on glucose uptake. Upon insulin exposure, PDK-1 membrane persistence was significantly reduced in L6IRƒ´43 compared to control cells. In L6 cells expressing IRWT, the C-terminal peptide also impaired insulin-dependent PDK-1 membrane persistence. Thus, PDK-1 directly binds to the insulin receptor, followed by PDK-1 activation and insulin metabolic effects. (literal)
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